Table of Contents
International Journal of Carbohydrate Chemistry
Volume 2016, Article ID 4760548, 42 pages
http://dx.doi.org/10.1155/2016/4760548
Review Article

Biosynthesis and Biological Activity of Carbasugars

Facultad de Química, Departamento de Química Orgánica, Universidad Complutense, Ciudad Universitaria, 28040 Madrid, Spain

Received 13 March 2016; Accepted 15 May 2016

Academic Editor: Sławomir Jarosz

Copyright © 2016 Silvia Roscales and Joaquín Plumet. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. L. de Paz and P. H. Seeberger, “Recent advances in carbohydrate microarrays,” QSAR and Combinatorial Science, vol. 25, no. 11, pp. 1027–1032, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. M. Miljkovic, Carbohydrates: Synthesis, Mechanisms, and Stereoelectronic Effects, Springer, 2010.
  3. R. V. Stick and S. J. Williams, Carbohydrates: The Essential Molecules of Life, Elsevier, New York, NY, USA, 2nd edition, 2009.
  4. M. Sinnott, Ed., Carbohydrate Chemistry and Biochemistry: Structure and Mechanism, RSC, 1st edition, 2007, 2nd edition, 2013.
  5. “Chemical reviews,” Carbohydrate Chemistry, vol. 10, no. 12, Edited by J. K. Bashkin, 2000.
  6. D. B. Werz and S. Vidal, Eds., Modern Synthetic Methods in Carbohydrate Chemistry. From Monosaccharides to Complex Glycoconjugates, John Wiley & Sons, New York, NY, USA, 2013.
  7. P. Kovac, Ed., Carbohydrate Chemistry. Proven Synthetic Methods, vol. 1, CRC Press. Taylor & Francis Group, 2011.
  8. G. van der Mare and J. Coreen, Eds., Carbohydrate Chemistry. Proven Synthetic Methods, vol. 2, CRC Press. Taylor & Francis Group, 2014.
  9. R. Roy and S. Vidal, Eds., Carbohydrate Chemistry. Proven Synthetic Methods, vol. 3, CRC Press. Taylor & Francis Group, 2015.
  10. Y. C. Lee and R. T. Lee, Eds., Recognition of Carbohydrates in Biological Systems. Part A: General Procedures, vol. 362 of Methods in Enzymology, Academic Press, New York, NY, USA, 2003.
  11. Y. C. Lee and R. T. Lee, Eds., Recognition of Carbohydrates in Biological Systems. Part B: Specific Applications, vol. 363 of Methods in Enzymology, Academic Press, New York, NY, USA, 2003.
  12. B. Wang and G. J. Boons, Eds., Carbohydrate Recognition. Biological Problems, Methods and Applications, Wileyohn Wiley & Sons, Bew York, NY, USA, 2011.
  13. P. H. Seeberger and Ch. Rademacher, Eds., Carbohydrates as Drugs, vol. 12 of Topics in Medicinal Chemistry, Springer, 2014.
  14. J. Jiménez-Barbero, J. Cañada, and S. Martín-Santamaría, Eds., Carbohydrates in Drug Design and Discovery, vol. 43, RSC: Drug Discovery Series, 2015.
  15. R. A. Dwek and T. D. Butters, “Introduction: glycobiology—understanding the language and meaning of carbohydrates,” Chemical Reviews, vol. 102, no. 2, pp. 283–284, 2002. View at Publisher · View at Google Scholar
  16. H. Lis and N. Sharon, “Lectins: carbohydrate-specific proteins that mediate cellular recognition,” Chemical Reviews, vol. 98, no. 2, pp. 637–674, 1998. View at Publisher · View at Google Scholar · View at Scopus
  17. V. L. Campo, V. Aragón-Leoneti, M. B. M. Teixeira, and I. Carvalho, “Carbohydrates and glycoproteins: cellular recognition and drug design,” New Developments in Medicinal Chemistry, vol. 1, pp. 133–151, 2010. View at Google Scholar
  18. L. L. Kiessling and J. C. Grim, “Glycopolymer probes of signal transduction,” Chemical Society Reviews, vol. 42, no. 10, pp. 4476–4491, 2013. View at Publisher · View at Google Scholar · View at Scopus
  19. Y.-L. Ruan, “Sucrose metabolism: gateway to diverse carbon use and sugar signaling,” Annual Review of Plant Biology, vol. 65, pp. 33–67, 2014. View at Publisher · View at Google Scholar · View at Scopus
  20. K. Ljung, J. L. Nemhauser, and P. Perata, “New mechanistic links between sugar and hormone signalling networks,” Current Opinion in Plant Biology, vol. 25, pp. 130–137, 2015. View at Publisher · View at Google Scholar
  21. J. M. Rini and H. Leffler, “Carbohydrate recognition and signaling,” in Functioning of Transmembrane Receptors in Signaling Mechanism, R. Bradshaw and E. A. Dennis, Eds., Cell Signaling Collection, chapter 13, pp. 341–347, Academic Press, New York, NY, USA, 2011. View at Google Scholar
  22. K. J. Doores, D. P. Gamblin, and B. G. Davis, “Exploring and exploiting the therapeutic potential of glycoconjugates,” Chemistry—A European Journal, vol. 12, no. 3, pp. 656–665, 2006. View at Publisher · View at Google Scholar · View at Scopus
  23. K. M. Koeller and C. H. Wong, “The concept of ‘Medicinal Glycoscience’ was developed,” in Emerging Themes in Medicinal Glycoscience, vol. 18 of Nature Biotechnology, pp. 835–841, 2000. View at Google Scholar
  24. S. J. Keding and S. J. Danishefsky, “Synthetic carbohydrate-based vaccines,” in Carbohydrate-Based Drug Discovery, C.-H. Wong, Ed., chapter 14, pp. 381–406, John Wiley & Sons, New York, NY, USA, 2003. View at Publisher · View at Google Scholar
  25. M.-L. Hecht, P. Stallforth, D. V. Silva, A. Adibekian, and P. H. Seeberger, “Recent advances in carbohydrate-based vaccines,” Current Opinion in Chemical Biology, vol. 13, no. 3, pp. 354–359, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. L. Morelli, L. Poletti, and L. Lay, “Carbohydrates and immunology: synthetic oligosaccharide antigens for vaccine formulation,” European Journal of Organic Chemistry, vol. 2011, no. 29, pp. 5723–5777, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. S. Bhatia, M. Dimde, and R. Haag, “Multivalent glycoconjugates as vaccines and potential drug candidates,” MedChemComm, vol. 5, no. 7, pp. 862–878, 2014. View at Publisher · View at Google Scholar · View at Scopus
  28. S. J. Danishefsky and J. R. Allen, “From the laboratory to the clinic: a retrospective on fully synthetic carbohydrate-based anticancer vaccines,” Angewandte Chemie International Edition, vol. 39, no. 5, pp. 836–863, 2000. View at Publisher · View at Google Scholar · View at Scopus
  29. “Part I: biosynthesis, structural diversity and sialoglycopathologies. Part II: tools and technique to identify and capture sialoglycans,” in Sialo Glyco Chemistry and Biology, R. Gerardy-Schahn, P. Delannoy, and M. von Itzstein, Eds., vol. 366-367 of Topics in Current Chemistry, Springer, Berlin, Germany, 2015.
  30. M. Pudelko, J. Bull, and H. Kunz, “Chemical and chemoenzymatic synthesis of glycopeptide selectin ligands containing sialyl Lewis X structures,” ChemBioChem, vol. 11, no. 7, pp. 904–930, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. N. Kaila and B. E. Thomas IV, “Design and synthesis of sialyl Lewisx mimics as E- and P-selectin inhibitors,” Medicinal Research Reviews, vol. 22, no. 6, pp. 566–601, 2002. View at Publisher · View at Google Scholar · View at Scopus
  32. A. L. Majumder and B. B. Biswas, Eds., Biology of Inositols and Phosphoinositides, vol. 39 of Subcellular Biochemistry, Springer, New York, NY, USA, 2006. View at Publisher · View at Google Scholar
  33. A. Kukisis, “Laboratory techniques in biochemistry and molecular biology,” in Inositol Phospholipid Metabolism and Phosphatidyl Inositol Kimases, S. Pillai and P. C. Van der Viet, Eds., chapter 5, pp. 253–334, Elsevier, New York, NY, USA, 2003. View at Google Scholar
  34. A. K. Menon, P. Orlean, T. Kinoshita, and F. Tamanoi, Eds., Glycosylphosphatidylinositols (GPI) Anchoring of Proteins, vol. 26 of The Enzimes, Elsevier, 2009.
  35. GPI, Membrane Anchors. The Much Needed Link, Edited by J. A. Dangerfield, Ch. Metamer, Bentham, 2010.
  36. I. Vilotijevic, S. Gutze, P. H. Seeberger, and D. V. Silva, “Chemical synthesis of GPI anchors and GPI anchored molecules,” in Modern Synthetic Methods in Carbohydrate Chemistry, D. B. Werz and S. Vidal, Eds., pp. 335–372, John Wiley & Sons, New York, NY, USA, 2014. View at Google Scholar
  37. Ch. Zurzolo and K. Simons, “Glycosylphosphatidylinositol-anchored proteins. Membrane, organization and transport,” Biochimica et Biophysica Acta (BBA)—Biomembranes, vol. 1858, no. 4, pp. 632–639, 2016. View at Publisher · View at Google Scholar
  38. G. H. Boons and K. J. Hale, Organic Synthesis with Carbohydrates, Wiley-Blackwell, 2000.
  39. M. M. K. Boysen, Ed., Carbohydrates Tools for Stereoselective Synthesis, John Wiley & Sons, Berlin, Germany, 2013.
  40. P. Sears and C.-H. Wong, “Carbohydrate mimetics: a new strategy for tackling the problem of carbohydrate-mediated biological recognition,” Angewandte Chemie—International Edition, vol. 38, no. 16, pp. 2300–2324, 1999. View at Publisher · View at Google Scholar · View at Scopus
  41. S. A. W. Gruner, E. Locardi, E. Lohof, and H. Kessler, “Carbohydrate-based mimetics in drug design: sugar amino acids and carbohydrate scaffolds,” Chemical Reviews, vol. 102, no. 2, pp. 491–514, 2002. View at Publisher · View at Google Scholar · View at Scopus
  42. D. C. Koester, A. Holkenbrink, and D. B. Werz, “Recent advances in the synthesis of carbohydrate mimetics,” Synthesis, no. 19, Article ID E27110SS, pp. 3217–3242, 2010. View at Publisher · View at Google Scholar · View at Scopus
  43. L. Cipolla and F. Peri, “Carbohydrate-based bioactive compounds for medicinal chemistry applications,” Mini-Reviews in Medicinal Chemistry, vol. 11, no. 1, pp. 39–54, 2011. View at Publisher · View at Google Scholar · View at Scopus
  44. Joint Commission on Biochemical Nomenclature, “Nomenclature of carbohydrates,” Pure and Applied Chemistry, vol. 68, pp. 1919–2008, 1996. View at Google Scholar
  45. O. Arjona, A. M. Gómez, J. C. López, and J. Plumet, “Synthesis and conformational and biological aspects of carbasugars,” Chemical Reviews, vol. 107, no. 5, pp. 1919–2036, 2007. View at Publisher · View at Google Scholar · View at Scopus
  46. J. Plumet, A. M. Gómez, and J. C. López, “Synthesis of carbasugars based on ring closing metathesis: 2000–2006,” Mini-Reviews in Organic Chemistry, vol. 4, no. 3, pp. 201–216, 2007. View at Publisher · View at Google Scholar · View at Scopus
  47. S. Jarosa, M. Nowogrodzki, M. Magdyca, and M. Potopnyk, “Carbobicyclic sugar mimics,” Journal of Carbohydrate Chemistry, vol. 37, pp. 303–325, 2012. View at Google Scholar
  48. R. G. Soengas, J. M. Otero, A. M. Estévez et al., “An overview of key routes for the transformation of sugars into carbasugars and related compounds,” Carbohydrate Chemistry, vol. 38, pp. 263–302, 2012. View at Publisher · View at Google Scholar · View at Scopus
  49. R. Lahiri, A. A. Ansari, and Y. D. Vankar, “Recent developments in design and synthesis of bicyclic azasugars, carbasugars and related molecules as glycosidase inhibitors,” Chemical Society Reviews, vol. 42, no. 12, pp. 5102–5118, 2013. View at Publisher · View at Google Scholar · View at Scopus
  50. M. Bessières, F. Chevrier, V. Roy, and L. A. Agrofoglio, “Recent progress for the synthesis of selected carbocyclic nucleosides,” Future Medicinal Chemistry, vol. 7, no. 13, pp. 1809–1828, 2015. View at Publisher · View at Google Scholar · View at Scopus
  51. P. Merino, Ed., Chemical Synthesis of Nucleoside Analogues, John Wiley & Sons, New York, NY, USA, 2013.
  52. M. Adinolfi, M. M. Corsaro, C. De Castro et al., “Caryose: a carbocyclic monosaccharide from Pseudomonas caryophylli,” Carbohydrate Research, vol. 284, no. 1, pp. 111–118, 1996. View at Publisher · View at Google Scholar · View at Scopus
  53. M. Adinolfi, M. M. Corsaro, C. De Castro et al., “Analysis of the polysaccharide components of the lipopolysaccharide fraction of Pseudomonas caryophylli,” Carbohydrate Research, vol. 284, no. 1, pp. 119–133, 1996. View at Publisher · View at Google Scholar · View at Scopus
  54. M. Adinolfi, G. Barone, A. Iadonisi, L. Mangoni, and R. Manna, “Synthesis of caryose, the carbocyclic monosaccharide component of the lipopolysaccharide from pseudomonas caryophylli,” Tetrahedron, vol. 53, no. 34, pp. 11767–11780, 1997. View at Publisher · View at Google Scholar · View at Scopus
  55. T. D. Brock, K. M. Brock, R. T. Belly, and R. L. Weiss, “Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature,” Archiv für Mikrobiologie, vol. 84, no. 1, pp. 54–68, 1972. View at Publisher · View at Google Scholar · View at Scopus
  56. M. de Rosa, S. de Rosa, A. Gambacorta, L. Minale, and J. D. Bullock, “Chemical structure of the ether lipids of thermophilic acidophilic bacteria of the Caldariella group,” Phytochemistry, vol. 16, no. 12, pp. 1961–1965, 1977. View at Publisher · View at Google Scholar · View at Scopus
  57. M. De Rosa, S. De Rosa, A. Gambacorta, and J. D. Bu'Lockt, “Structure of calditol, a new branched-chain nonitol, and of the derived tetraether lipids in thermoacidophile archaebacteria of the Caldariella group,” Phytochemistry, vol. 19, no. 2, pp. 249–254, 1980. View at Publisher · View at Google Scholar · View at Scopus
  58. M. L. Bode, S. R. Buddoo, S. H. Minnaar, and C. A. du Plessis, “Extraction, isolation and NMR data of the tetraether lipid calditoglycerocaldarchaeol (GDNT) from Sulfolobus metallicus harvested from a bioleaching reactor,” Chemistry and Physics of Lipids, vol. 154, no. 2, pp. 94–104, 2008. View at Publisher · View at Google Scholar · View at Scopus
  59. É. Untersteller, B. Fritz, Y. Bliériot, and P. Sinaÿ, “The structure of calditol isolated from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius,” Comptes Rendus de l'Academie des Sciences—Series IIC-Chemistry, vol. 2, no. 7-8, pp. 429–433, 1999. View at Publisher · View at Google Scholar · View at Scopus
  60. Y. Blériot, E. Untersteller, B. Fritz, and P. Sinaÿ, “Total synthesis of calditol: structural clarification of this typical component of Archaea order Sulfolobales,” Chemistry, vol. 8, no. 1, pp. 240–246, 2002. View at Google Scholar · View at Scopus
  61. T. W. Miller, B. H. Arison, and G. Albers Schonberg, “Isolation of a cyclitol antibiotic: 2,3,4,5-tetrahydroxycyclohexanemethanol,” Biotechnology and Bioengineering, vol. 15, no. 6, pp. 1075–1080, 1973. View at Publisher · View at Google Scholar · View at Scopus
  62. J. Marco-Contelles, M. T. Molina, and S. Anjum, “Naturally occurring cyclohexane epoxides: sources, biological activities, and synthesis,” Chemical Reviews, vol. 104, no. 6, pp. 2857–2899, 2004. View at Publisher · View at Google Scholar · View at Scopus
  63. C. Thebtaranonth and Y. Thebtaranonth, “Naturally occurring cyclohexene oxides,” Accounts of Chemical Research, vol. 19, no. 3, pp. 84–90, 1986. View at Publisher · View at Google Scholar · View at Scopus
  64. J. Marco-Contelles, “Cyclohexane epoxides—chemistry and biochemistry of (+)-cyclophellitol,” European Journal of Organic Chemistry, no. 9, pp. 1607–1618, 2001. View at Google Scholar · View at Scopus
  65. Y. Kobayashi, Glycoscience, Chemistry and Chemical Biology, vol. 3, chapter 10.3, Springer, Berlin, Germany, 2001.
  66. K. Tatsuta, “Total synthesis and chemical design of useful glycosidase inhibitors,” Pure and Applied Chemistry, vol. 68, no. 6, pp. 1341–1346, 1996. View at Google Scholar · View at Scopus
  67. S. Ogawa and M. Kanto, “Synthesis of bio-active compounds from cyclitol derivatives provided by bioconversion of myo-inositol,” Current Trends in Medicinal Chemistry, vol. 5, pp. 1–13, 2008. View at Google Scholar
  68. B. Fraser-Reid and J. C. López, “Unsaturated sugars: a rich platform for methodological and synthetic studies,” Current Organic Chemistry, vol. 13, no. 6, pp. 532–553, 2009. View at Publisher · View at Google Scholar · View at Scopus
  69. Y. Nobuji, C. Noriko, M. Takashi, U. Shigeru, A. Kenzon, and I. Michaki, “Novel herbicidal MK7607 and its manufacture with Curvularia,” Japanese Kokai Tokkyo Koho, JP, 06306000, 1994.
  70. A. Isogai, S. Sakuda, J. Nakayama, S. Watanabe, and A. Suzuki, “Isolation and structural elucidation of a new cyclitol derivative, streptol, as a plant growth regulator,” Agricultural and Biological Chemistry, vol. 51, no. 8, pp. 2277–2279, 1987. View at Publisher · View at Google Scholar · View at Scopus
  71. P. Sedmera, P. Halada, and S. Pospisil, “New carbasugars from Streptomyces lincolnensis,” Magnetic Resonance in Chemistry, vol. 47, no. 6, pp. 519–522, 2009. View at Publisher · View at Google Scholar
  72. T. Yamada, M. Iritani, H. Ohishi et al., “Pericosines, antitumour metabolites from the sea hare-derived fungus Periconia byssoides. Structures and biological activities,” Organic and Biomolecular Chemistry, vol. 5, no. 24, pp. 3979–3986, 2007. View at Publisher · View at Google Scholar · View at Scopus
  73. V. Usami, “Synthesis of marine-derived carbasugar pericosines,” Studies in Natural Products Chemistry, vol. 41, pp. 287–319, 2014. View at Google Scholar
  74. P. Bayón and M. Figueredo, “The gabosine and anhydrogabosine family of secondary metabolites,” Chemical Reviews, vol. 113, no. 7, pp. 4680–4707, 2013. View at Publisher · View at Google Scholar · View at Scopus
  75. D. H. Mac, S. Chandrasekhar, and R. Grée, “Total synthesis of gabosines,” European Journal of Organic Chemistry, no. 30, pp. 5881–5895, 2012. View at Publisher · View at Google Scholar · View at Scopus
  76. M. Das and K. Manna, “Bioactive cyclohexenones: a mini review,” Current Bioactive Compounds, vol. 11, no. 4, pp. 239–248, 2015. View at Publisher · View at Google Scholar
  77. H. Chimura, H. Nakamura, T. Takita et al., “The structure of a glyoxalase I inhibitor and its chemical reactivity with SH-compounds,” The Journal of Antibiotics, vol. 28, no. 10, pp. 743–748, 1975. View at Publisher · View at Google Scholar · View at Scopus
  78. S. Horii, T. Iwasa, and Y. Kameda, “Studies on validamycins, new antibiotics. V. Degradation studies,” The Journal of Antibiotics, vol. 24, no. 1, pp. 57–58, 1971. View at Publisher · View at Google Scholar · View at Scopus
  79. S. Horii, T. Iwasa, E. Mizuta, and Y. Kameda, “Studies on validamycins, new antibiotics. VI. Validamine, hydroxyvalidamine and validatol, new cyclitols,” Journal of Antibiotics, vol. 24, no. 1, pp. 59–63, 1971. View at Publisher · View at Google Scholar · View at Scopus
  80. Y. Kameda, N. Asano, M. Yoshikawa et al., “Valiolamine, a new α-glucosidase inhibiting aminocyclitol produced by Streptomyces hygroscopicus,” The Journal of Antibiotics, vol. 37, no. 11, pp. 1301–1307, 1984. View at Publisher · View at Google Scholar · View at Scopus
  81. Y. Kameda and S. Horii, “The unsaturated cyclitol part of the new antibiotics, the validamycins,” Journal of the Chemical Society, Chemical Communications, no. 12, pp. 746–747, 1972. View at Publisher · View at Google Scholar · View at Scopus
  82. Y. Kameda, S. Horii, and T. Yamano, “Microbial transformation of validamycins,” Journal of Antibiotics, vol. 28, no. 4, pp. 298–306, 1975. View at Publisher · View at Google Scholar · View at Scopus
  83. Y. Kameda, N. Asano, M. Teranishi, and K. Matsui, “New cyclitols, degradation of validamycin A by Flavobacterium saccharophilum,” Journal of Antibiotics, vol. 33, no. 12, pp. 1573–1574, 1980. View at Publisher · View at Google Scholar · View at Scopus
  84. Y. Kameda, N. Asano, M. Teranishi, M. Yoshikawa, and K. Matsui, “New intermediates, degradation of validamycin a by Flavobacterium saccharophilum,” The Journal of Antibiotics, vol. 34, no. 9, pp. 1237–1240, 1981. View at Publisher · View at Google Scholar
  85. N. Asano, M. Takeuchi, K. Ninomiya, Y. Kameda, and K. Matsui, “Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A,” Journal of Antibiotics, vol. 37, no. 8, pp. 859–867, 1984. View at Publisher · View at Google Scholar · View at Scopus
  86. S. Ogawa, Y. Miyamoto, and A. Nakajima, “Cleavage of the imino bonds of validoxylamine A derivatives with N-bromosuccinimide,” Chemistry Letters, pp. 725–728, 1989. View at Google Scholar
  87. S. Ogawa, A. Nakajima, and Y. Miyamoto, “Cleavage of validoxylamine A derivatives with N-bromosuccinimide: preparation of blocked synthons useful for the construction of carba-oligosaccharides composed of imino linkages,” Journal of the Chemical Society, Perkin Transactions, vol. 1, no. 12, pp. 3287–3290, 1991. View at Google Scholar · View at Scopus
  88. H. Xu, J. Yang, L. Bai, Z. Deng, and T. Mahmud, “Genetically engineered production of 1,1′-bis-valienamine and validienamycin in Streptomyces hygroscopicus and their conversion to valienamine,” Applied Microbiology and Biotechnology, vol. 81, no. 5, pp. 895–902, 2009. View at Publisher · View at Google Scholar · View at Scopus
  89. Y.-P. Xue, Y.-G. Zheng, and Y.-C. Shen, “Enhanced production of valienamine by Stenotrophomonas maltrophilia with fed-batch culture in a stirred tank bioreactor,” Process Biochemistry, vol. 42, no. 6, pp. 1033–1038, 2007. View at Publisher · View at Google Scholar · View at Scopus
  90. Y.-S. Wang, Y.-G. Zheng, and Y.-C. Shen, “Isolation and identification of a novel valienamine-producing bacterium,” Journal of Applied Microbiology, vol. 102, no. 3, pp. 838–844, 2007. View at Publisher · View at Google Scholar · View at Scopus
  91. T. Mahmud, “The C7N aminocyclitol family of natural products,” Natural Product Reports, vol. 20, no. 1, pp. 137–166, 2003. View at Publisher · View at Google Scholar · View at Scopus
  92. T. Suami, “Synthesis of biologically active pseudo-oligosaccharides,” in Carbohydrates, H. Ogura, A. Hasegawa, and T. Suami, Eds., pp. 136–173, VCH, 1992. View at Google Scholar
  93. T. Iwasa, H. Yamamoto, and M. Shibata, “Studies on validamycins, new antibiotics. I. Streptomyces hygroscopicus var. limoneus nov. var., validamycin-producing organism,” Journal of Antibiotics, vol. 23, no. 12, pp. 595–602, 1970. View at Publisher · View at Google Scholar · View at Scopus
  94. T. Iwasa, E. Higashide, H. Yamamoto, and M. Shibata, “Studies on validamycins, new antibiotics. II. Production and biological properties of validamycins A and B,” Journal of Antibiotics, vol. 24, no. 2, pp. 107–113, 1971. View at Publisher · View at Google Scholar · View at Scopus
  95. S. Horii, Y. Kameda, and K. Kawahara, “Studies on validamycins, new antibiotics. 8. Isolation and characterization of validamycins C,D,E and F.,” Journal of Antibiotics, vol. 25, no. 1, pp. 48–53, 1972. View at Publisher · View at Google Scholar · View at Scopus
  96. Y. Kameda, N. Asano, K. Matsui, S. Horii, and H. Fukase, “Structures of minor components of the validamycin complex,” Journal of Antibiotics, vol. 41, no. 10, pp. 1488–1492, 1988. View at Publisher · View at Google Scholar · View at Scopus
  97. Y. Kameda, N. Asano, T. Yamaguchi, K. Matsui, S. Horii, and H. Fukase, “Validamycin G and validoxylamine G, new members of the validamycins,” Journal of Antibiotics, vol. 39, no. 10, pp. 1491–1494, 1986. View at Publisher · View at Google Scholar · View at Scopus
  98. N. Asano, Y. Kameda, K. Matsui, S. Horii, and H. Fukase, “Validamycin H, a new pseudo-tetrasaccharide antibiotic,” The Journal of Antibiotics, vol. 43, no. 8, pp. 1039–1041, 1990. View at Publisher · View at Google Scholar · View at Scopus
  99. D. D. Schmidt, W. Frommer, B. Junge et al., “α-Glucosidase inhibitors—new complex oligosaccharides of microbial origin,” Naturwissenschaften, vol. 64, no. 10, pp. 535–536, 1977. View at Publisher · View at Google Scholar · View at Scopus
  100. B. Junge, F.-R. Heiker, J. Kurz, L. Müller, D. D. Schmidt, and C. Wünsche, “Untersuchungen zur struktur des α-d-glucosidaseinhibitors acarbose,” Carbohydrate Research, vol. 128, no. 2, pp. 235–268, 1984. View at Publisher · View at Google Scholar · View at Scopus
  101. U. Masharani and M. S. German, “Pancreatic hormones and diabetes mellitus,” in Greenspan's Basic & Clinical Endocrinology, D. G. Gardner and D. Shoback, Eds., chapter 17, McGraw-Hill Medical, 9th edition, 2011. View at Google Scholar
  102. J. B. Buse, K. S. Polonsky, and Ch. F. Burant, “Type 2 diabetes mellitus,” in Williams Textbook of Endocrinology, S. Melmed, K. S. Polonsky, P. R. Larsen, and H. M. Kronenberg, Eds., section 7, chapter 31, Elsevier, 12th edition, 2012. View at Google Scholar
  103. A. Kadziola, J.-I. Abe, B. Svensson, and R. Haser, “Crystal and molecular structure of barley α-amylase,” Journal of Molecular Biology, vol. 239, no. 1, pp. 104–121, 1994. View at Publisher · View at Google Scholar · View at Scopus
  104. M. Machius, G. Wiegand, and R. Huber, “Crystal structure of calcium-depleted Bacillus licheniformisα-amylase at 2.2 Å resolution,” Journal of Molecular Biology, vol. 246, no. 4, pp. 545–559, 1995. View at Publisher · View at Google Scholar · View at Scopus
  105. M. Hemker, A. Stratmann, K. Goeke et al., “Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50,” Journal of Bacteriology, vol. 183, no. 15, pp. 4484–4492, 2001. View at Publisher · View at Google Scholar · View at Scopus
  106. E. Truscheit, W. Frommer, B. Junge, L. Muller, D. Schmidt, and W. Wingeder, “Chemistry and biochemistry of microbial α-glucosidase inhibitors,” Angewandte Chemie—International Edition, vol. 20, no. 9, pp. 744–761, 1981. View at Publisher · View at Google Scholar · View at Scopus
  107. U. F. Wehmeier and W. Piepersberg, “Biotechnology and molecular biology of the α-glucosidase inhibitor acarbose,” Applied Microbiology and Biotechnology, vol. 63, no. 6, pp. 613–625, 2004. View at Publisher · View at Google Scholar · View at Scopus
  108. U. F. Wehmeier, “The biosynthesis and metabolism of acarbose in Actinoplanes sp. SE 50/110: a progress report,” Biocatalysis and Biotransformation, vol. 21, no. 4-5, pp. 279–284, 2003. View at Publisher · View at Google Scholar · View at Scopus
  109. H. Laube, “Acarbose. An update of its therapeutic use in diabetes treatment,” Clinical Drug Investigation, vol. 22, no. 3, pp. 141–156, 2002. View at Publisher · View at Google Scholar · View at Scopus
  110. A. J. Scheen, “Clinical efficacy of acarbose in diabetes mellitus: a critical review of controlled trials,” Diabetes and Metabolism, vol. 24, no. 4, pp. 311–321, 1998. View at Google Scholar · View at Scopus
  111. H.-W. M. Breuer, “Review of acarbose therapeutic strategies in the long-term treatment and in the prevention of type 2 diabetes,” International Journal of Clinical Pharmacology and Therapeutics, vol. 41, no. 10, pp. 421–440, 2003. View at Publisher · View at Google Scholar · View at Scopus
  112. S. Ogawa, M. Kanto, and Y. Suzuki, “Development and medical application of unsaturated carbaglycosylamine glycosidase inhibitors,” Mini-Reviews in Medicinal Chemistry, vol. 7, no. 7, pp. 679–691, 2007. View at Publisher · View at Google Scholar · View at Scopus
  113. A. Bedekar, K. Shah, and M. Koffas, “Natural products for type II diabetes treatment,” Advances in Applied Microbiology, vol. 71, pp. 21–73, 2010. View at Publisher · View at Google Scholar · View at Scopus
  114. J. L. Ríos, F. Francini, and G. R. Schinella, “Natural products for the treatment of type 2 diabetes mellitus,” Planta Medica, vol. 81, no. 12-13, pp. 975–994, 2015. View at Publisher · View at Google Scholar · View at Scopus
  115. A. L. Harvey, “Plant natural products in anti-diabetic drug discovery,” Current Organic Chemistry, vol. 14, no. 16, pp. 1670–1677, 2010. View at Publisher · View at Google Scholar · View at Scopus
  116. N. S. H. N. Moorthy, M. J. Ramos, and P. A. Fernandes, “Studies on α-glucosidase inhibitors development: magic molecules for the treatment of carbohydrate mediated diseases,” Mini-Reviews in Medicinal Chemistry, vol. 12, no. 8, pp. 713–720, 2012. View at Publisher · View at Google Scholar · View at Scopus
  117. U. Ghani, “Re-exploring promising α-glucosidase inhibitors for potential development into oral anti-diabetic drugs: finding needle in the haystack,” European Journal of Medicinal Chemistry, vol. 103, pp. 133–162, 2015. View at Publisher · View at Google Scholar · View at Scopus
  118. K.-I. Fukuhara, H. Murai, and S. Murao, “Amylostatins, other amylase inhibitors produced by Streptomyces diastaticus subsp. Amylostaticus No. 2476,” Agricultural and Biological Chemistry, vol. 46, no. 8, pp. 2021–2030, 1982. View at Google Scholar
  119. K. Fukuhara, H. Murai, and S. Murao, “Isolation and structure-activity relationship of some amylostatins (F-1b fraction) produced by Streptomyces diastaticus subsp. Amylostaticus No. 9410,” Agricultural and Biological Chemistry, vol. 46, no. 7, pp. 1941–1945, 1982. View at Google Scholar · View at Scopus
  120. S. Namiki, K. Kangouri, T. Nagate, H. Hara, K. Sugita, and S. Omura, “Studies on the α-glucoside hydrolase inhibitor, adiposin. I. Isolation and physicochemical properties,” The Journal of Antibiotics, vol. 35, no. 9, pp. 1234–1236, 1982. View at Publisher · View at Google Scholar · View at Scopus
  121. S. Namiki, K. Kangouri, T. Nagate, H. Hara, K. Sugita, and S. Omura, “Studies on the α-glucoside hydrolase inhibitor, adiposin. II. Taxonomic studies on the producing microorganism,” The Journal of Antibiotics, vol. 35, no. 9, pp. 1156–1159, 1982. View at Publisher · View at Google Scholar · View at Scopus
  122. K. Kangouri, S. Namiki, T. Nagate, H. Hara, K. Sugita, and S. Omura, “Studies on the α-glucoside hydrolase inhibitor, adiposin. III. α-Glucoside hydrolase inhibitory activity and antibacterial activity in vitro,” The Journal of Antibiotics, vol. 35, no. 9, pp. 1160–1166, 1982. View at Publisher · View at Google Scholar · View at Scopus
  123. S. Namiki, K. Kangouri, T. Nagate et al., “Studies on the α-glucoside hydrolase inhibitor, adiposin. IV. Effect of adiposin on intestinal digestion of carbohydrates in experimental animals,” Journal of Antibiotics, vol. 35, no. 9, pp. 1167–1173, 1982. View at Publisher · View at Google Scholar · View at Scopus
  124. S. Ogawa, Y. Iwasawa, T. Toyokuni, and T. Suami, “Synthesis of adiposin-1, α-glucoside hydrolase inhibitor,” Chemistry Letters, vol. 12, no. 3, pp. 337–340, 1983. View at Publisher · View at Google Scholar
  125. S. Ogawa, Y. Iwasawa, T. Toyokuni, and T. Suami, “Synthesis of pseudooligosaccharidic glycosidase inhibitors. Part 1. Synthesis ofadiposin-1 and related compounds,” Carbohydrate Research, vol. 141, pp. 29–40, 1985. View at Google Scholar
  126. S. Ogawa and Y. Shibata, “Total synthesis of acarbose andadiposin-2,” Journal of the Chemical Society, Chemical Communications, no. 9, pp. 605–606, 1988. View at Publisher · View at Google Scholar
  127. Y. Shibata and S. Ogawa, “Synthesis of pseudo-oligosaccharide glycosidase inhibitors. Part VII. Total synthesis of acarbose andadiposin-2,” Carbohydrate Research, vol. 189, pp. 309–322, 1989. View at Publisher · View at Google Scholar
  128. J. Itoh, S. Omoto, T. Shomura et al., “Oligostatins, new antibiotics with amylase inhibitory activity. I. Production, isolation and characterization,” Journal of Antibiotics, vol. 34, no. 11, pp. 1424–1428, 1981. View at Publisher · View at Google Scholar · View at Scopus
  129. S. Omoto, J. Itoh, H. Ogino, K. Iwamatsu, N. Nishizawa, and S. Inouye, “Oligostatins, new antibiotics with amylase inhibitory activity. II. Structures of oligostatins C, D and E,” The Journal of Antibiotics, vol. 34, no. 11, pp. 1429–1433, 1981. View at Publisher · View at Google Scholar · View at Scopus
  130. S. Ogawa, Y. Iwasawa, T. Toyokuni, and T. Suami, “Synthesis of a common structural unit of the antibiotic oligostatins,” Chemistry Letters, vol. 11, no. 11, pp. 1729–1732, 1982. View at Publisher · View at Google Scholar
  131. S. Ogawa, Y. Iwasawa, T. Toyokuni, and T. Suami, “Synthesis of a core structure of the antibiotic oligostatin,” Carbohydrate Research, vol. 144, no. 1, pp. 155–162, 1985. View at Publisher · View at Google Scholar
  132. Y. Shibata, Y. Kosuge, and S. Ogawa, “Synthesis and biological activities of methyl oligobiosaminide and some deoxy isomers thereof,” Carbohydrate Research, vol. 199, no. 1, pp. 37–54, 1990. View at Publisher · View at Google Scholar · View at Scopus
  133. K. Watanabe, T. Furumai, M. Sudoh, K. Yokose, and H. B. Maruyama, “New α-amylase inhibitor, trestatins. IV. Taxonomy of the producing strains and fermentation of trestatin A,” Journal of Antibiotics, vol. 37, no. 5, pp. 479–486, 1984. View at Publisher · View at Google Scholar · View at Scopus
  134. K. Yokose, K. Ogawa, T. Sano, K. Watanabe, H.-B. Maruyama, and Y. Suhara, “New α-amylase inhibitor, trestatins. I. Isolation, characterization and biological activities of trestatins A, B and C,” The Journal of Antibiotics, vol. 36, no. 9, pp. 1157–1165, 1983. View at Publisher · View at Google Scholar · View at Scopus
  135. L. Vértesy, H.-W. Fehlhaber, and A. Schulz, “The trehalase inhibitor salbostatin, a novel metabolite from Streptomyces albus, ATCC 21838,” Angewandte Chemie—International Edition, vol. 33, no. 18, pp. 1844–1846, 1994. View at Publisher · View at Google Scholar · View at Scopus
  136. T. Yamagishi, Ch. Uchida, and S. Ogawa, “Total synthesis of the trehalase inhibitor salbostatin,” Chemistry: A European Journal, vol. 1, pp. 634–636, 1996. View at Google Scholar
  137. T. Yamagishi, Ch. Uchida, and S. Ogawa, “Total synthesis of trehalase inhibitor salbostatin,” Bioorganic & Medicinal Chemistry Letters, vol. 5, no. 5, pp. 487–490, 1995. View at Publisher · View at Google Scholar · View at Scopus
  138. N. Kawamura, N. Kinoshita, R. Sawa et al., “Pyralomicins, novel antibiotics from Microtetraspora spiralis. I. Taxonomy and production,” The Journal of Antibiotics, vol. 49, no. 7, pp. 706–709, 1996. View at Publisher · View at Google Scholar · View at Scopus
  139. N. Kawamura, R. Sawa, Y. Rakahashi et al., “Pyralomicins, new antibiotics from Actinomadura spiralis,” Journal of Antibiotics, vol. 48, no. 5, pp. 435–437, 1995. View at Publisher · View at Google Scholar · View at Scopus
  140. N. Kawamura, R. Sawa, Y. Takahashi et al., “Pyralomicins, novel antibiotics from Microtetraspora spiralis. II. Structure determination,” Journal of Antibiotics, vol. 49, no. 7, pp. 651–656, 1996. View at Publisher · View at Google Scholar · View at Scopus
  141. T. R. Kelly and R. L. Moiseyeva, “Total synthesis of the pyralomicinones,” Journal of Organic Chemistry, vol. 63, no. 9, pp. 3147–3150, 1998. View at Publisher · View at Google Scholar · View at Scopus
  142. K. Tatsuta, M. Takahashi, and N. Tanaka, “The first total synthesis of pyralomicin 2c,” Tetrahedron Letters, vol. 40, no. 10, pp. 1929–1932, 1999. View at Publisher · View at Google Scholar · View at Scopus
  143. K. Tatsuta, M. Takahashi, and N. Tanaka, “The first total synthesis of pyralomicin 1c,” Journal of Antibiotics, vol. 53, no. 1, pp. 88–91, 2000. View at Publisher · View at Google Scholar · View at Scopus
  144. G. N. Jenkins and N. J. Turner, “The biosynthesis of carbocyclic nucleosides,” Chemical Society Reviews, vol. 24, no. 3, pp. 169–176, 1995. View at Publisher · View at Google Scholar · View at Scopus
  145. R. J. Parry, “Investigations of the biosynthesis of aristeromycin,” in Secondary-Metabolite Biosynthesis and Metabolism, vol. 44 of Environmental Science Research, pp. 89–104, Springer, Berlin, Germany, 1992. View at Publisher · View at Google Scholar
  146. J. M. Hill, G. N. Jenkins, C. P. Rush et al., “Revised pathway for the biosynthesis of aristeromycin and neplanocin A from D-glucose in Streptomyces citricolor,” Journal of the American Chemical Society, vol. 117, no. 19, pp. 5391–5392, 1995. View at Publisher · View at Google Scholar · View at Scopus
  147. R. J. Parry and Y. Jiang, “The biosynthesis of aristeromycin. Conversion of neplanocin A to aristeromycin by a novel enzymatic reduction,” Tetrahedron Letters, vol. 35, no. 52, pp. 9665–9668, 1994. View at Publisher · View at Google Scholar · View at Scopus
  148. A. Gambacorta, A. Gliozzi, and M. De Rosa, “Archaeal lipids and their biotechnological applications,” World Journal of Microbiology and Biotechnology, vol. 11, no. 1, pp. 115–131, 1995. View at Publisher · View at Google Scholar
  149. A. Gambacorta, G. Caracciolo, D. Trabasso, I. Izzo, A. Spinella, and G. Sodano, “Biosynthesis of calditol, the cyclopentanoid containing moiety of the membrane lipids of the archaeon Sulfolobus solfataricus,” Tetrahedron Letters, vol. 43, no. 3, pp. 451–453, 2002. View at Publisher · View at Google Scholar · View at Scopus
  150. N. Yamauchi, H. Ueoka, N. Kamada, and T. Murae, “Resemblance of carbocycle formation from carbohydrates between archaea and eucarya/eubacteria. Biosynthesis of calditol, the characteristic lipid-content molecule in Sulfolobus acidocaldarius,” Bulletin of the Chemical Society of Japan, vol. 77, no. 4, pp. 771–778, 2004. View at Publisher · View at Google Scholar
  151. N. Yamauchi, N. Kamada, and H. Ueoka, “The possibility of involvement of ‘cyclase’ enzyme of the calditol carbocycle with broad substrate specificity in Sulfolobus acidcaldarius, a typical thermophilic archaea,” Chemistry Letters, vol. 35, no. 11, pp. 1230–1231, 2006. View at Publisher · View at Google Scholar · View at Scopus
  152. B. Nicolaus, A. Trincone, E. Esposito, M. R. Vaccaro, A. Gambacorta, and M. De Rosa, “Calditol tetraether lipids of the archaebacterium Sulfolobus solfataricus. Biosynthetic studies,” Biochemical Journal, vol. 266, no. 3, pp. 785–791, 1990. View at Google Scholar · View at Scopus
  153. D. Voet and J. G. Voet, “Citric acid cycle,” in Biochemistry, chapter 21, John Wiley & Sons, New York, NY, USA, 3rd edition, 2004. View at Google Scholar
  154. J. M. Berg, J. L. Tymoczko, and L. Stryer, Biochemistry, W. H. Freeman, San Francisco, Calif, USA, 5th edition, 2002.
  155. S. Singh, A. Anand, and P. K. Srivastava, “Regulation and properties of glucose-6-phosphate dehydrogenase: a review,” International Journal of Plant Physiology and Biochemistry, vol. 4, pp. 1–19, 2012. View at Google Scholar
  156. H. W. Hofer and H. P. Bauer, “6-Phosphogluconolactonase,” Cell Biochemistry and Function, vol. 5, no. 2, pp. 97–99, 1987. View at Publisher · View at Google Scholar · View at Scopus
  157. M. Rippa, S. Hanau, C. Cervellati, and F. Dallocchio, “6-Phosphogluconate dehydrogenase: structural symmetry and functional asymmetry,” Protein and Peptide Letters, vol. 7, no. 5, pp. 341–348, 2000. View at Google Scholar · View at Scopus
  158. W. T. Williamson and W. A. Wood, “D-Ribulose-5-phosphate3-epimerase,” Methods in Enzymology, vol. 9, pp. 605–608, 1966. View at Google Scholar
  159. T. Wood, “Assay for D-ribose-5-phosphate ketol isomerase and D-ribulose-5-phosphate 3-epimerase,” Methods in Enzymology, vol. 41, pp. 63–66, 1975. View at Publisher · View at Google Scholar · View at Scopus
  160. G. A. Kochetov and O. N. Solovjeva, “Structure and functioning mechanism of transketolase,” Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics, vol. 1844, no. 9, pp. 1608–1618, 2014. View at Publisher · View at Google Scholar · View at Scopus
  161. A. Ranoux and U. Hanefeld, “Improving transketolase,” Topics in Catalysis, vol. 56, no. 9-10, pp. 750–764, 2013. View at Publisher · View at Google Scholar · View at Scopus
  162. R. Wohlgemuth, M. E. B. Smith, P. A. Dalby, and J. M. Woodley, “Transketolases,” in Encyclopedia of Industrial, M. C. Flickinger, Ed., vol. 7, pp. 4746–4752, John Wiley & Sons, New York, NY, USA, 2010. View at Google Scholar
  163. T. Widlanski, S. L. Bender, and J. R. Knowles, “Dehydroquinate synthase: a sheep in wolf's clothing?” Journal of the American Chemical Society, vol. 111, no. 6, pp. 2299–2300, 1989. View at Publisher · View at Google Scholar · View at Scopus
  164. A. Stratmann, T. Mahmud, S. Lee, J. Distler, H. G. Floss, and W. Piepersberg, “The AcbC protein from actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the α-glucosidase inhibitor acarbose,” The Journal of Biological Chemistry, vol. 274, no. 16, pp. 10889–10896, 1999. View at Publisher · View at Google Scholar · View at Scopus
  165. S. Asamizu, P. Xie, C. J. Brumsted, P. M. Flatt, and T. Mahmud, “Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to several distinct cyclic products,” Journal of the American Chemical Society, vol. 134, no. 29, pp. 12219–12229, 2012. View at Publisher · View at Google Scholar · View at Scopus
  166. K. M. Kean, S. J. Codding, S. Asamizu, T. Mahmud, and P. A. Karplus, “Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus,” Biochemistry, vol. 53, no. 26, pp. 4250–4260, 2014. View at Publisher · View at Google Scholar · View at Scopus
  167. E. P. Carpenter, A. R. Hawkins, J. W. Frost, and K. A. Brown, “Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis,” Nature, vol. 394, no. 6690, pp. 299–302, 1998. View at Publisher · View at Google Scholar · View at Scopus
  168. K. M. Herrmann, “The shikimate pathway: early steps in the biosynthesis of aromatic compounds,” Plant Cell, vol. 7, no. 7, pp. 907–919, 1995. View at Publisher · View at Google Scholar · View at Scopus
  169. R. Höfs, S. Schoppe, R. Thiericke, and A. Zeeck, “Biosynthesis of gabosines A, B, and C, carba sugars from Streptomyces cellulosae,” European Journal of Organic Chemistry, vol. 2000, no. 10, pp. 1883–1887, 2000. View at Google Scholar · View at Scopus
  170. S. Y. Liu and J. P. N. Rosazza, “Enzymatic conversion of glucose to UDP-4-keto-6-deoxyglucose in Streptomyces spp.,” Applied and Environmental Microbiology, vol. 64, no. 10, pp. 3972–3976, 1998. View at Google Scholar · View at Scopus
  171. C. J. Thibodeaux, C. E. Melançon, and H.-W. Liu, “Unusual sugar biosynthesis and natural product glycodiversification,” Nature, vol. 446, no. 7139, pp. 1008–1016, 2007. View at Publisher · View at Google Scholar · View at Scopus
  172. M. Á. Fresneda, R. Alibés, J. Font, P. Bayón, and M. Figueredo, “How a diversity-oriented approach has inspired a new hypothesis for the gabosine biosynthetic pathway. A new synthesis of (+)-gabosine C,” Organic and Biomolecular Chemistry, vol. 11, no. 38, pp. 6562–6568, 2013. View at Publisher · View at Google Scholar · View at Scopus
  173. R. Alibés, P. Bayón, P. De March, M. Figueredo, J. Font, and G. Marjanet, “Enantioselective synthesis and absolute configuration assignment of gabosine O. synthesis of (+)- and (-)-gabosine N and (+)- and (-)-epigabosines N and O,” Organic Letters, vol. 8, no. 8, pp. 1617–1620, 2006. View at Publisher · View at Google Scholar · View at Scopus
  174. H. Dong, T. Mahmud, I. Tornus, S. Lee, and H. G. Floss, “Biosynthesis of the validamycins: identification of intermediates in the biosynthesis of validamycin A by Streptomyces hygroscopicus var. limoneus,” Journal of the American Chemical Society, vol. 123, no. 12, pp. 2733–2742, 2001. View at Publisher · View at Google Scholar · View at Scopus
  175. S.-H. Lee, H. Choe, K. S. Bae, D.-S. Park, A. Nasir, and K. M. Kim, “Complete genome of Streptomyces hygroscopicus subsp. limoneus KCTC 1717 (=KCCM 11405), a soil bacterium producing validamycin and diverse secondary metabolites,” Journal of Biotechnology, vol. 219, pp. 1–2, 2016. View at Publisher · View at Google Scholar · View at Scopus
  176. S. Lee and E. Egelkrout, “Biosynthetic studies on the α-glucosidase inhibitor acarbose in Actinoplanes sp.: glutamate is the primary source of the nitrogen in acarbose,” Journal of Antibiotics, vol. 51, no. 2, pp. 225–227, 1998. View at Publisher · View at Google Scholar · View at Scopus
  177. M. K. Patterson Jr. and G. R. Orr, “Asparagine biosynthesis by the Novikoff Hepatoma. Isolation, purification, property, and mechanism studies of the enzyme system,” The Journal of Biological Chemistry, vol. 243, no. 2, pp. 376–380, 1968. View at Google Scholar · View at Scopus
  178. A. R. Tesson, T. S. Soper, M. Ciustea, and N. G. J. Richards, “Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli,” Archives of Biochemistry and Biophysics, vol. 413, no. 1, pp. 23–31, 2003. View at Publisher · View at Google Scholar · View at Scopus
  179. T. Mahmud, S. Lee, and H. G. Floss, “The biosynthesis of acarbose and validamycin,” Chemical Records, vol. 1, no. 4, pp. 300–310, 2001. View at Publisher · View at Google Scholar · View at Scopus
  180. K. Arakawa, S. G. Bowers, B. Michels, V. Trin, and T. Mahmud, “Biosynthetic studies on the α-glucosidase inhibitor acarbose: the chemical synthesis of isotopically labeled 2-epi-5-epi-valiolone analogs,” Carbohydrate Research, vol. 338, no. 20, pp. 2075–2082, 2003. View at Publisher · View at Google Scholar · View at Scopus
  181. T. Mahmud, I. Tornus, E. Egelkrout et al., “Biosynthetic studies on the α-glucosidase inhibitor acarbose in Actinoplanes sp.: 2-epi-5-epi-valiolone is the direct precursor of the valienamine moiety,” Journal of the American Chemical Society, vol. 121, no. 30, pp. 6973–6983, 1999. View at Publisher · View at Google Scholar · View at Scopus
  182. A. M. Coghill and L. R. Garson, Eds., The ACS Style Guide: Effective Communication of Scientific Diphosphates Information, American Chemical Society, Washington, DC, USA, 3rd edition, 2006.
  183. Q. Cui, W. S. Shin, Y. Luo, J. Tian, H. Cui, and D. Yin, “Thymidylate kinase: an old topic brings new perspectives,” Current Medicinal Chemistry, vol. 20, no. 10, pp. 1286–1305, 2013. View at Publisher · View at Google Scholar · View at Scopus
  184. S. Lee, B. Sauerbrei, J. Niggemann, and E. Egelkrout, “Biosynthetic studies on the α-glucosidase inhibitor acarbose in Actinoplanes sp.: source of the maltose unit,” The Journal of Antibiotics, vol. 50, no. 11, pp. 954–960, 1997. View at Publisher · View at Google Scholar · View at Scopus
  185. S. G. Bowers, T. Mahmud, and H. G. Floss, “Biosynthetic studies on the α-glucosidase inhibitor acarbose: the chemical synthesis of dTDP-4-amino-4,6-dideoxy-α-D-glucose,” Carbohydrate Research, vol. 337, no. 4, pp. 297–304, 2002. View at Publisher · View at Google Scholar · View at Scopus
  186. U. F. Wehmeier and W. Piepersberg, “Enzymology of aminoglycoside biosynthesis-deduction from gene cluster,” in Complex Enzymes in Microbial Natural Products Biosynthesis. Part B.: Polyketides, Aminocoumarins and Carbohydrates, D. A. Howood, Ed., vol. 459 of Methods in Enzymology, chapter 19, p. 479, Elsevier, 2009. View at Google Scholar
  187. H. Lodish, A. Berk, Ch. Kaiser et al., “Genes, genomics and chromosomes,” in Molecular Cell Biology, pp. 227–230, Freeman, 7th edition, 2013. View at Google Scholar
  188. G. Yi, S.-H. Sze, and M. R. Thon, “Identifying clusters of functionally related genes in genomes,” Bioinformatics, vol. 23, no. 9, pp. 1053–1060, 2007. View at Publisher · View at Google Scholar · View at Scopus
  189. R. Overbeek, M. Fonstein, M. D'Souza, G. D. Push, and N. Maltsev, “The use of gene clusters to infer functional coupling,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 6, pp. 2896–2901, 1999. View at Publisher · View at Google Scholar · View at Scopus
  190. J. Yang, H. Xu, Y. Zhang, L. Bai, Z. Deng, and T. Mahmud, “Nucleotidylation of unsaturated carbasugar in validamycin biosynthesis,” Organic and Biomolecular Chemistry, vol. 9, no. 2, pp. 438–449, 2011. View at Publisher · View at Google Scholar · View at Scopus
  191. Ch.-S. Zhang, M. Podeschwa, O. Block, H.-J. Altenbach, W. Piepersberg, and U. F. Wehmeier, “Identification of a 1-epi-vañienol 7-kinase activity in the producer of acarbose, Actinoplanes sp. SE50/110,” FEBS Letters, vol. 540, no. 1–3, pp. 53–57, 2003. View at Publisher · View at Google Scholar · View at Scopus
  192. C.-S. Zhang, A. Stratmann, O. Block et al., “Biosynthesis of the C7-cyclitol moiety of acarbose in Actinoplanes species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor leads to proposal of a new biosynthetic pathway,” The Journal of Biological Chemistry, vol. 277, no. 25, pp. 22853–22862, 2002. View at Publisher · View at Google Scholar · View at Scopus
  193. A. Stratmann, T. Mahmud, S. Lee, J. Distler, H. G. Floss, and W. Piepersberg, “The AcbC protein from Actinoplanes species is a C7-cyclitol synthase related to 3-dehydroquinate synthases and is involved in the biosynthesis of the α-glucosidase inhibitor acarbose,” Journal of Biological Chemistry, vol. 274, no. 16, pp. 10889–10896, 1999. View at Publisher · View at Google Scholar · View at Scopus
  194. S. Wendler, V. Ortseifen, M. Persicke et al., “Carbon source dependent biosynthesis of acarviose metabolites in Actinoplanes sp. SE50/110,” Journal of Biotechnology, vol. 191, pp. 113–120, 2014. View at Publisher · View at Google Scholar · View at Scopus
  195. D. E. Metzler, Biochemistry. The Chemical Reactions of Living Cells, vol. 1, Elsevier, 2nd edition, 2003.
  196. P. M. Flatt, X. Wu, S. Perry, and T. Mahmud, “Genetic insights into pyralomicin biosynthesis in Nonomuraea spiralis IMC A-0156,” Journal of Natural Products, vol. 76, no. 5, pp. 939–946, 2013. View at Publisher · View at Google Scholar · View at Scopus
  197. D. Schwarzer, R. Finking, and M. A. Marahiel, “Nonribosomal peptides: from genes to products,” Natural Product Reports, vol. 20, no. 3, pp. 275–287, 2003. View at Publisher · View at Google Scholar · View at Scopus
  198. M. A. Marahiel, T. Stachelhaus, and H. D. Mootz, “Modular peptide synthetases involved in nonribosomal peptide synthesis,” Chemical Reviews, vol. 97, no. 7, pp. 2651–2673, 1997. View at Publisher · View at Google Scholar · View at Scopus
  199. C. Khosla, R. S. Gokhale, J. R. Jacobsen, and D. E. Cane, “Tolerance and specificity of polyketide synthases,” Annual Review of Biochemistry, vol. 68, pp. 219–253, 1999. View at Publisher · View at Google Scholar · View at Scopus
  200. H. Jenke-Kodama, A. Sandmann, R. Müller, and E. Dittmann, “Evolutionary implications of bacterial polyketide synthases,” Molecular Biology and Evolution, vol. 22, no. 10, pp. 2027–2039, 2005. View at Publisher · View at Google Scholar · View at Scopus
  201. H. Lodish, L. Zipursky, P. B. Matsudaira, D. David, and J. Darnel, Molecular Definition of a Gene—Molecular Cell Biology, W. H. Freeman, San Francisco, Calif, USA, 2000.
  202. G. J. Williams, “Engineering polyketide synthases and nonribosomal peptide synthetases,” Current Opinion in Structural Biology, vol. 23, no. 4, pp. 603–612, 2003. View at Publisher · View at Google Scholar
  203. C. R. Hutchinson, “Polyketide and non-ribosomal peptide synthases: falling together by coming apart,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 6, pp. 3010–3012, 2003. View at Publisher · View at Google Scholar
  204. M. E. Horsman, T. P. A. Hari, and Ch. N. Boddy, “Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?” Natural Product Reports, vol. 33, no. 2, pp. 183–202, 2016. View at Publisher · View at Google Scholar · View at Scopus
  205. D. R. M. Smith, S. Grüschow, and R. J. Goss, “Scope and potential of halogenases in biosynthetic applications,” Current Opinion in Chemical Biology, vol. 17, no. 2, pp. 276–283, 2013. View at Publisher · View at Google Scholar · View at Scopus
  206. T. Bureau, K. C. Lam, R. K. Ibrahim, B. Behdad, and S. Dayanandan, “Structure, function, and evolution of plant O-methyltransferases,” Genome, vol. 50, no. 11, pp. 1001–1013, 2007. View at Publisher · View at Google Scholar · View at Scopus
  207. S. Singh, G. N. Phillips Jr., and J. S. Thorson, “The structural biology of enzymes involved in natural product glycosylation,” Natural Product Reports, vol. 29, no. 10, pp. 1201–1237, 2012. View at Publisher · View at Google Scholar · View at Scopus
  208. A. Chang, S. Singh, G. N. Phillips, and J. S. Thorson, “Glycosyltransferase structural biology and its role in the design of catalysts for glycosylation,” Current Opinion in Biotechnology, vol. 22, no. 6, pp. 800–808, 2011. View at Publisher · View at Google Scholar · View at Scopus
  209. H. Nothaft and C. M. Szymanski, “Protein glycosylation in bacteria: sweeter than ever,” Nature Reviews Microbiology, vol. 8, no. 11, pp. 765–778, 2010. View at Publisher · View at Google Scholar · View at Scopus
  210. D. Calo, L. Kaminski, and J. Eichler, “Protein glycosylation in Archaea: sweet and extreme,” Glycobiology, vol. 20, no. 9, pp. 1065–1076, 2010. View at Publisher · View at Google Scholar · View at Scopus
  211. W. S. Choi, X. Wu, Y.-H. Choeng et al., “Genetic organization of the putative salbostatin biosynthetic gene cluster including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus ATCC 21838,” Applied Microbiology and Biotechnology, vol. 80, no. 4, pp. 637–645, 2008. View at Publisher · View at Google Scholar · View at Scopus
  212. G. E. McCasland, S. Furuta, and L. J. Durham, “Alicyclic carbohydrates. XXIX. The synthesis of a pseudo-hexose (2,3,4,5-tetrahydroxycyclohexanemethanol),” Journal of Organic Chemistry, vol. 31, no. 5, pp. 1516–1521, 1966. View at Publisher · View at Google Scholar · View at Scopus
  213. T. Suami, S. Ogawa, M. Takata et al., “Synthesis of sweet tasting pseudo-β-fructopyranose,” Chemistry Letters, vol. 14, no. 6, pp. 719–722, 1985. View at Publisher · View at Google Scholar
  214. T. Suami, S. Ogawa, M. Takata, K. Yasuda, K. Takei, and A. Suga, “Pseudo-sugars. XIV. Synthesis of sweet-tasting pseudo-β-dl-fructopyranose,” Bulletin of the Chemical Society of Japan, vol. 59, no. 3, pp. 819–821, 1986. View at Publisher · View at Google Scholar
  215. S. Ogawa, Y. Uematsu, and S. Yoshida, “Synthesis and sweetness of pseudo-β-D and L-fructopyranose,” Journal of Carbohydrate Chemistry, vol. 6, no. 3, pp. 471–478, 1987. View at Publisher · View at Google Scholar · View at Scopus
  216. J. M. Berg, J. L. Tymoczko, and L. Stryer, Biochemistry, chapter 8, section 8.5, Freeman, 5th edition, 2002.
  217. U. Etxeberria, A. L. de la Garza, J. Campión, J. A. Martínez, and F. I. Milagro, “Antidiabetic effects of natural plant extracts via inhibition of carbohydrate hydrolysis enzymes with emphasis on pancreatic alpha amylase,” Expert Opinion on Therapeutic Targets, vol. 16, no. 3, pp. 269–297, 2012. View at Publisher · View at Google Scholar · View at Scopus
  218. R. J. Parry, M. R. Burns, P. N. Skae, J. C. Hoyt, and B. Pal, “Carbocyclic analogues of D-ribose-5-phosphate: synthesis and behavior with 5-phosphoribosyl α-1-pyrophosphate synthetases,” Bioorganic and Medicinal Chemistry, vol. 4, no. 7, pp. 1077–1088, 1996. View at Publisher · View at Google Scholar · View at Scopus
  219. J. H. Kim, D. Wolle, K. Haridas, R. J. Parry, J. L. Smith, and H. Zalkin, “A stable carbocyclic analog of 5-phosphoribosyl-1-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase,” The Journal of Biological Chemistry, vol. 270, no. 29, pp. 17394–17399, 1995. View at Publisher · View at Google Scholar · View at Scopus
  220. R. J. Parry and K. Haridas, “Synthesis of 1α-Pyrophosphoryl-2α,3α-dihydroxy-4β-cyclopentanemethanol-5-phosphate, a Carbocyclic Analog of 5-Phosphoribosyl-1-pyrophosphate (PRPP),” Tetrahedron Letters, vol. 34, no. 44, pp. 7013–7016, 1993. View at Publisher · View at Google Scholar · View at Scopus
  221. J. A. Duley, J. Christodoulou, and A. P. M. de Brouwer, “The PRPP synthetase spectrum: what does it demonstrate about nucleotide syndromes?” Nucleosides, Nucleotides & Nucleic Acids, vol. 30, no. 12, pp. 1129–1139, 2011. View at Publisher · View at Google Scholar · View at Scopus
  222. M. Tatibana, K. Kita, M. Taira et al., “Mammalian phosphoribosyl-pyrophosphate synthetase,” Advances in Enzyme Regulation, vol. 35, pp. 229–249, 1995. View at Publisher · View at Google Scholar · View at Scopus
  223. S. Fujimori, “Genetic bases of gout and hyperuricemia. I. PRPP synthetase superactivity,” in Genetic Errors Associated with Purine and Pyrimidine Metabolism in Humans: Diagnosis and Treatment, Y. Moriwaki and T. Yamamoto, Eds., pp. 6–14, Research Signpost, Thiruvananthapuram, India, 2006. View at Google Scholar
  224. United States Food, Drug Administration, and Guidance for Industry, Drug Interaction Studies-Study Design, Data Analysis, and Implications for Dosing and Labeling, Clinical Pharmacology, 2006.
  225. M. A. Becker, P. R. Smith, W. Taylor, R. Mustafi, and R. L. Switzer, “The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity,” Journal of Clinical Investigation, vol. 96, no. 5, pp. 2133–2141, 1995. View at Publisher · View at Google Scholar · View at Scopus
  226. S. Mazurek, C. B. Boschek, and E. Eigenbrodt, “The role of phosphometabolites in cell proliferation, energy metabolism, and tumor therapy,” Journal of Bioenergetics and Biomembranes, vol. 29, no. 4, pp. 315–330, 1997. View at Publisher · View at Google Scholar · View at Scopus
  227. M. Sunamura, M. Oonuma, F. Motoi et al., “Gene therapy for pancreatic cancer targeting the genomic alterations of tumor suppressor genes using replication-selective oncolytic adenovirus,” Human Cell, vol. 15, no. 3, pp. 138–150, 2002. View at Google Scholar · View at Scopus
  228. J. R. K. Cairns and A. Esen, “β-Glucosidases,” Cellular and Molecular Life Sciences, vol. 67, no. 20, pp. 3389–3405, 2010. View at Publisher · View at Google Scholar · View at Scopus
  229. K. Tatsuta, “Total synthesis and chemical design of useful glycosidase inhibitors,” in Carbohydrate Mimics, Y. Chapleur, Ed., pp. 283–305, John Wiley & Sons, New York, NY, USA, 1998. View at Google Scholar
  230. W. W. Kallemeijn, M. D. Witte, T. Wennekes, and J. M. F. G. Aerts, “Mechanism-based inhibitors of glycosidases: design and applications,” Advances in Carbohydrate Chemistry and Biochemistry, vol. 71, pp. 297–338, 2014. View at Publisher · View at Google Scholar · View at Scopus
  231. S. Atsumi, H. Iinuma, C. Nosaka, and K. Umezawa, “Biological activities of cyclophellitol,” The Journal of Antibiotics, vol. 43, no. 12, pp. 1579–1585, 1990. View at Publisher · View at Google Scholar · View at Scopus
  232. S. Pengthaisong, C.-F. Chen, S. G. Withers, B. Kuaprasert, and J. R. Ketudat Cairns, “Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition,” Carbohydrate Research, vol. 352, pp. 51–59, 2012. View at Publisher · View at Google Scholar · View at Scopus
  233. T. M. Gloster, R. Madsen, and G. J. Davies, “Structural basis for cyclophellitol inhibition of a β-glucosidase,” Organic & Biomolecular Chemistry, vol. 5, no. 3, pp. 444–446, 2007. View at Publisher · View at Google Scholar · View at Scopus
  234. M. Nakata, C. Chong, Y. Niwata, K. Toshima, and K. Tatsuta, “A family of cyclophellitol analogs: synthesis and evaluation,” Journal of Antibiotics, vol. 46, no. 12, pp. 1919–1922, 1993. View at Publisher · View at Google Scholar · View at Scopus
  235. V. W.-F. Tai, P.-H. Fung, Y.-S. Wong, and T. K. M. Shing, “Synthesis and glycosidase-inhibitory activity of cyclophellitol analogues,” Tetrahedron: Asymmetry, vol. 5, no. 7, pp. 1353–1362, 1994. View at Publisher · View at Google Scholar · View at Scopus
  236. V. W.-F. Tai, P.-H. Fung, Y.-S. Wong, and T. K. M. Shing, “Kinetic studies on cyclophellitol analogues—mechanism-based inactivators,” Biochemical and Biophysical Research Communications, vol. 213, no. 1, pp. 175–180, 1995. View at Publisher · View at Google Scholar · View at Scopus
  237. K.-Y. Li, J. Jiang, M. D. Witte et al., “Exploring functional cyclophellitol analogues as human retaining beta-glucosidase inhibitors,” Organic & Biomolecular Chemistry, vol. 12, no. 39, pp. 7786–7791, 2014. View at Publisher · View at Google Scholar · View at Scopus
  238. K. Tatsuta, Y. Niwata, K. Umezawa, K. Toshima, and M. Nakata, “Enantiospecific synthesis and biological evaluation of 1,6-epi-cyclophellitol,” Journal of Antibiotics, vol. 44, no. 4, pp. 456–458, 1991. View at Publisher · View at Google Scholar · View at Scopus
  239. S. Atsumi, C. Nosaka, Y. Ochi, H. Iinuma, and K. Umezawa, “Inhibition of experimental metastasis by an α-glucosidase inhibitor, 1,6-epi-cyclophellitol,” Cancer Research, vol. 53, no. 20, pp. 4896–4899, 1993. View at Google Scholar · View at Scopus
  240. W. W. Kallemeijn, K.-Y. Li, M. D. Witte et al., “Novel activity-based probes for broad-spectrum profiling of retaining β-exoglucosidases in situ and in vivo,” Angewandte Chemie—International Edition, vol. 51, no. 50, pp. 12529–12533, 2012. View at Publisher · View at Google Scholar · View at Scopus
  241. K.-Y. Li, J. Jiang, M. D. Witte et al., “Synthesis of cyclophellitol, cyclophellitol aziridine, and their tagged derivatives,” European Journal of Organic Chemistry, vol. 2014, no. 27, pp. 6030–6043, 2014. View at Publisher · View at Google Scholar · View at Scopus
  242. L. I. Willems, T. J. M. Beenakker, B. Murray et al., “Synthesis of α- and β-galactopyranose-configured isomers of cyclophellitol and cyclophellitol aziridine,” European Journal of Organic Chemistry, vol. 2014, no. 27, pp. 6044–6056, 2014. View at Publisher · View at Google Scholar · View at Scopus
  243. J. Jiang, T. J. M. Beenakker, W. W. Kallemeijn et al., “Comparing cyclophellitol N-alkyl and N-acyl cyclophellitol aziridines as activity-based glycosidase probes,” Chemistry, vol. 21, no. 30, pp. 10861–10869, 2015. View at Publisher · View at Google Scholar · View at Scopus
  244. T. Suami and S. Ogawa, “Chemistry of carba-sugars (pseudo-sugars) and their derivatives,” Advances in Carbohydrate Chemistry and Biochemistry, vol. 48, pp. 21–90, 1990. View at Publisher · View at Google Scholar · View at Scopus
  245. K. Kamata, M. Mitsuya, T. Nishimura, J.-I. Eiki, and Y. Nagata, “Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase,” Structure, vol. 12, no. 3, pp. 429–438, 2004. View at Publisher · View at Google Scholar · View at Scopus
  246. C. Postic, M. Shiota, and M. A. Magnuson, “Cell-specific roles of glucokinase in glucose homeostasis,” Recent Progress in Hormone Research, vol. 56, pp. 195–217, 2001. View at Publisher · View at Google Scholar · View at Scopus
  247. I. Miwa, H. Hara, J. Okuda, T. Suami, and S. Ogawa, “Inhibition of glucose-stimulated insulin release by pseudo-α- DL-glucose as a glucokinase inhibitor,” Biochemistry International, vol. 11, no. 6, pp. 809–816, 1985. View at Google Scholar · View at Scopus
  248. M. Kitaoka, S. Ogawa, and H. Taniguchi, “A cellobiose phosphorylase from Cellvibrio gilvus recognizes only the β-d-form of 5a-carba-glucopyranose,” Carbohydrate Research, vol. 247, pp. 355–359, 1993. View at Publisher · View at Google Scholar · View at Scopus
  249. Y. Sugimoto, H. Suzuki, H. Yamaki, T. Nishimura, and N. Tanaka, “Mechanism of action of 2-crotonyloxymethyl-4,5,6-trihydroxycyclohex-2-enone, a SH inhibitory antitumor antibiotic, and its effect on drug-resistant neoplastic cells,” Journal of Antibiotics, vol. 35, no. 9, pp. 1222–1230, 1982. View at Publisher · View at Google Scholar · View at Scopus
  250. C. F. M. Huntley, D. S. Hamilton, D. J. Creighton, and B. Ganem, “Reaction of COTC with glutathione: structure of the putative glyoxalase I inhibitor,” Organic Letters, vol. 2, no. 20, pp. 3143–3144, 2000. View at Publisher · View at Google Scholar · View at Scopus
  251. D. Kamiya, Y. Uchihata, E. Ichikawa, K. Kato, and K. Umezawa, “Reversal of anticancer drug resistance by COTC based on intracellular glutathione and glyoxalase I,” Bioorganic and Medicinal Chemistry Letters, vol. 15, no. 4, pp. 1111–1114, 2005. View at Publisher · View at Google Scholar · View at Scopus
  252. F. Collu, L. Bonsignore, M. Casu, C. Floris, J. Gertsch, and F. Cottiglia, “New cytotoxic saturated and unsaturated cyclohexanones from Anthemis maritima,” Bioorganic and Medicinal Chemistry Letters, vol. 18, no. 5, pp. 1559–1562, 2008. View at Publisher · View at Google Scholar · View at Scopus
  253. E. Joseph, J. L. Eiseman, D. S. Hamilton et al., “Molecular basis of the antitumor activities of 2-crotonyloxymethyl-2-cycloalkenones,” Journal of Medicinal Chemistry, vol. 46, no. 1, pp. 194–196, 2003. View at Publisher · View at Google Scholar · View at Scopus
  254. P. J. Thornalley, “Glyoxalase I—structure, function and a critical role in the enzymatic defence against glycation,” Biochemical Society Transactions, vol. 31, no. 6, pp. 1343–1348, 2003. View at Publisher · View at Google Scholar · View at Scopus
  255. D. J. Creighton and D. S. Hamilton, “Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations,” Archives of Biochemistry and Biophysics, vol. 387, no. 1, pp. 1–10, 2001. View at Publisher · View at Google Scholar · View at Scopus
  256. S. Mirza, L.-P. Molleyres, and A. Vasella, “Synthesis of a glyoxalase I inhibitor from Streptomyces griseosporeus Niida et Ogasawara,” Helvetica Chimica Acta, vol. 68, no. 4, pp. 988–996, 1985. View at Publisher · View at Google Scholar · View at Scopus
  257. H. Takayama, K. Hayashi, and T. Koizumi, “Enantioselective total synthesis of Glyoxalase I inhibitor using asymmetric Diels-Alder reaction of a new chiral dienophile, (S)S-3-(3-triflouromethylpyrid-2-ylsulfinyl)acrylate,” Tetrahedron Letters, vol. 27, no. 45, pp. 5509–5512, 1986. View at Publisher · View at Google Scholar · View at Scopus
  258. T. K. M. Shing and Y. Tang, “Enantiospecific synthesis of 2-crotonyloxy-(4R,5R,6R)-4,5,6-trihydroxycyclohex-2-enone (COTC) from quinic acid,” Journal of the Chemical Society, Chemical Communications, no. 4, p. 312, 1990. View at Publisher · View at Google Scholar · View at Scopus
  259. C. F. M. Huntley, H. B. Wood, and B. Ganem, “A new synthesis of the glyoxalase-I inhibitor COTC,” Tetrahedron Letters, vol. 41, no. 13, pp. 2031–2034, 2000. View at Publisher · View at Google Scholar · View at Scopus
  260. C. L. Arthurs, N. S. Wind, R. C. Whitehead, and I. J. Stratford, “Analogues of 2-crotonyloxymethyl-(4R,5R,6R)-4,5,6-trihydroxycyclohex-2-enone (COTC) with anti-tumor properties,” Bioorganic and Medicinal Chemistry Letters, vol. 17, no. 2, pp. 553–557, 2007. View at Publisher · View at Google Scholar · View at Scopus
  261. C. L. Arthurs, J. Raftery, H. L. Whitby, R. C. Whitehead, N. S. Wind, and I. J. Stratford, “Arene cis-dihydrodiols: useful precursors for the preparation of analogues of the anti-tumour agent, 2-crotonyloxymethyl-(4R,5R,6R)-4,5,6-trihydroxycyclohex-2-enone (COTC),” Bioorganic and Medicinal Chemistry Letters, vol. 17, no. 21, pp. 5974–5977, 2007. View at Publisher · View at Google Scholar · View at Scopus
  262. C. L. Arthurs, G. A. Morris, M. Piacenti et al., “The synthesis of 2-oxyalkyl-cyclohex-2-enones, related to the bioactive natural products COTC and antheminone A, which possess anti-tumour properties,” Tetrahedron, vol. 66, no. 46, pp. 9049–9060, 2010. View at Publisher · View at Google Scholar · View at Scopus
  263. T. K. M. Shing, H. T. Wu, H. F. Kwok, and C. B. S. Lau, “Synthesis of chiral hydroxylated enones as potential anti-tumor agents,” Bioorganic and Medicinal Chemistry Letters, vol. 22, no. 24, pp. 7562–7565, 2012. View at Publisher · View at Google Scholar · View at Scopus
  264. C. L. Arthurs, K. F. Lingley, M. Piacenti et al., “(-)-Quinic acid: a versatile precursor for the synthesis of analogues of 2-crotonyloxymethyl-(4R,5R,6R)-4,5,6-trihydroxycyclohex-2-enone (COTC) which possess anti-tumour properties,” Tetrahedron Letters, vol. 49, no. 15, pp. 2410–2413, 2008. View at Publisher · View at Google Scholar · View at Scopus
  265. P. M. Dowling, “Aminoglycosides and aminocyclitols,” in Antimicrobial Therapy in Veterinary Medicine, S. Giguère, J. F. Prescott, and P. M. Dowling, Eds., chapter 14, pp. 233–255, John Wiley & Sons, Hoboken, NJ, USA, 5th edition, 2013. View at Publisher · View at Google Scholar
  266. F. Kudo and T. Eguchi, “Aminoglycoside antibiotics: new insights into the biosynthetic machinery of old drugs,” The Chemical Record, vol. 16, no. 1, pp. 4–18, 2016. View at Publisher · View at Google Scholar
  267. N. M. Llewellyn and J. B. Spencer, “Biosynthesis of 2-deoxystreptamine-containing aminoglycoside antibiotics,” Natural Product Reports, vol. 23, no. 6, pp. 864–874, 2006. View at Publisher · View at Google Scholar · View at Scopus
  268. E. Nango, T. Eguchi, and K. Kakinuma, “Active site mapping of 2-deoxy-scyllo-inosose synthase, the key starter enzyme for the biosynthesis of 2-deoxystreptamine. Mechanism-based inhibition and identification of lysine-141 as the entrapped nucleophile,” Journal of Organic Chemistry, vol. 69, no. 3, pp. 593–600, 2004. View at Publisher · View at Google Scholar · View at Scopus
  269. D. Dykes and W. Waud, “Murine L1210 and P388 leukemias,” in Tumor Models in Cancer Research, B. Teicher, Ed., pp. 23–40, Humana Press, 2002. View at Google Scholar
  270. A. Numata, M. Iritani, T. Yamada et al., “Novel antitumour metabolites produced by a fungal strain from a sea hare,” Tetrahedron Letters, vol. 38, no. 47, pp. 8215–8218, 1997. View at Publisher · View at Google Scholar · View at Scopus
  271. R. S. Herbst, “Review of epidermal growth factor receptor biology,” International Journal of Radiation Oncology Biology Physics, vol. 59, no. 2, pp. 21–26, 2004. View at Publisher · View at Google Scholar · View at Scopus
  272. J. J. Chanpoux, “DNA topoisomerases: structure, function, and mechanism,” Annual Review of Biochemistry, vol. 70, pp. 369–413, 2001. View at Google Scholar
  273. G. Bach, S. Breiding-Mack, S. Grabley et al., “Secondary metabolites by chemical screening. 22. Gabosines, new carba-sugars from Streptomyces,” Liebigs Annalen der Chemie, pp. 241–250, 1993. View at Google Scholar
  274. N. B. Javitt, “Hep G2 cells as a resource for metabolic studies: lipoprotein, cholesterol, and bile acids,” The FASEB Journal, vol. 4, no. 2, pp. 161–168, 1990. View at Google Scholar · View at Scopus
  275. Y.-Q. Tang, C. Maul, R. Höfs et al., “Gabosines L, N and O: new carba-sugars from streptomyces with DNA-binding properties,” European Journal of Organic Chemistry, no. 1, pp. 149–153, 2000. View at Publisher · View at Google Scholar · View at Scopus
  276. A. Maier, C. Maul, M. Zerlin, S. Grabley, and R. Thiericke, “Biomolecular-chemical screening. A novel screening approach for the discovery of biologically active secondary metabolites. II. Application studies with pure metabolites,” The Journal of Antibiotics, vol. 52, no. 11, pp. 952–959, 1999. View at Publisher · View at Google Scholar · View at Scopus
  277. K. Tatsuta, T. Tsuchiya, N. Mikami, S. Umezawa, H. Umezawa, and H. Naganawa, “KD16 U1, a new metabolite of Streptomyces. Isolation and structural studies,” Journal of Antibiotics, vol. 27, no. 8, pp. 579–586, 1974. View at Publisher · View at Google Scholar · View at Scopus
  278. B. Winchester, “Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins,” Biochemical Society Transactions, vol. 12, no. 3, pp. 522–524, 1984. View at Publisher · View at Google Scholar · View at Scopus
  279. A. Vidyasagar and K. M. Sureshan, “Total synthesis and glycosidase inhibition studies of (-)-gabosine J and its derivatives,” European Journal of Organic Chemistry, vol. 2014, no. 11, pp. 2349–2356, 2014. View at Publisher · View at Google Scholar · View at Scopus
  280. O. F. Smetanina, A. I. Kalinovskii, Y. V. Khudyakov et al., “Metabolites of the marine fungus Asperigillus varians KMM 4630,” Chemistry of Natural Compounds, vol. 41, no. 2, pp. 243–244, 2005. View at Publisher · View at Google Scholar · View at Scopus
  281. K. Trisuwan, V. Rukachaisirikul, Y. Sukpondma et al., “Epoxydons and a pyrone from the marine-derived fungus Nigrospora sp. PSU-F5,” Journal of Natural Products, vol. 71, no. 8, pp. 1323–1326, 2008. View at Publisher · View at Google Scholar · View at Scopus
  282. S. Qin, H. Hussain, B. Schulz, S. Draeger, and K. Krohn, “Two new metabolites, epoxydine A and B, from Phoma sp.,” Helvetica Chimica Acta, vol. 93, no. 1, pp. 169–174, 2010. View at Publisher · View at Google Scholar · View at Scopus
  283. H. Kakeya, Y. Miyake, M. Shoji et al., “Novel non-peptide inhibitors targeting death receptor-mediated apoptosis,” Bioorganic & Medicinal Chemistry Letters, vol. 13, no. 21, pp. 3743–3746, 2003. View at Publisher · View at Google Scholar · View at Scopus
  284. T. Mitsui, Y. Miyake, H. Kakeya, Y. Hayashi, H. Osada, and T. Kataoka, “RKTS-33, an epoxycyclohexenone derivative that specifically inhibits Fas ligand-dependent apoptosis in CTL-mediated cytotoxicity,” Bioscience, Biotechnology and Biochemistry, vol. 69, no. 10, pp. 1923–1928, 2005. View at Publisher · View at Google Scholar · View at Scopus
  285. T. D. Gilmore, “Introduction to NF-κB: players, pathways, perspectives,” Oncogene, vol. 25, no. 51, pp. 6680–6684, 2006. View at Publisher · View at Google Scholar · View at Scopus
  286. A. R. Brasier, “The NF-κB regulatory network,” Cardiovascular Toxicology, vol. 6, no. 2, pp. 111–130, 2006. View at Publisher · View at Google Scholar · View at Scopus
  287. T. Saitoh, E. Suzuki, A. Takasugi et al., “Efficient synthesis of (±)-parasitenone, a novel inhibitor of NF-κB,” Bioorganic & Medicinal Chemistry Letters, vol. 19, no. 18, pp. 5383–5386, 2009. View at Publisher · View at Google Scholar · View at Scopus
  288. C.-H. Wang, H. T. Wu, H. M. Cheng et al., “Inhibition of glutathione S-Transferase M1 by new gabosine analogues is essential for overcoming cisplatin resistance in lung cancer cells,” Journal of Medicinal Chemistry, vol. 54, no. 24, pp. 8574–8581, 2011. View at Publisher · View at Google Scholar · View at Scopus
  289. D. J. Giard, S. A. Aaronson, G. J. Todaro et al., “In vitro cultivation of human tumors: establishment of cell lines derived from a series of solid tumors,” Journal of the National Cancer Institute, vol. 51, no. 5, pp. 1417–1423, 1973. View at Google Scholar · View at Scopus
  290. L. S. Engel, E. Taioli, R. Pfeiffer et al., “Pooled analysis and meta-analysis of glutathione S-transferase M1 and bladder cancer: a HuGE review,” American Journal of Epidemiology, vol. 156, no. 2, pp. 95–109, 2002. View at Publisher · View at Google Scholar · View at Scopus
  291. S. Ogawa, H. Aoyama, and T. Sato, “Synthesis of an ether-linked alkyl 5a-carba-β-D-glucoside, a 5a-carba-β-D-galactoside, a 2-acetamido-2-deoxy-5a-carba-β-D-glucoside, and an alkyl 5a′-carba-β-lactoside,” Carbohydrate Research, vol. 337, no. 21–23, pp. 1979–1992, 2002. View at Publisher · View at Google Scholar · View at Scopus
  292. J. C. Becker, R. Houben, D. Schrama, H. Voigt, S. Ugurel, and R. A. Reisfeld, “Mouse models for melanoma: a personal perspective,” Experimental Dermatology, vol. 19, no. 2, pp. 157–164, 2010. View at Publisher · View at Google Scholar · View at Scopus
  293. L. N. David and M. C. Michael, Lipids. Lehninger Principles of Biochemistry, W H Freeman, 4th edition, 2005.
  294. I. Mocchetti, “Exogenous gangliosides, neuronal plasticity and repair, and the neurotrophins,” Cellular and Molecular Life Sciences, vol. 62, no. 19-20, pp. 2283–2294, 2005. View at Publisher · View at Google Scholar · View at Scopus
  295. V. Jeanneret, P. Vogel, P. Renaut, J. Millet, J. Theveniaux, and V. Barberousse, “Carbaxylosides of 4-ethyl-2-oxo-2H-benzopyran-7-yl as non-hydrolyzable, orally active venous antithrombotic agents,” Bioorganic and Medicinal Chemistry Letters, vol. 8, no. 13, pp. 1687–1688, 1998. View at Publisher · View at Google Scholar · View at Scopus
  296. M. Lefoix, A. Tatibouët, S. Cottaz, H. Driguez, and P. Rollin, “Carba-glucotropaeolin: the first non-hydrolyzable glucosinolate analogue, to inhibit myrosinase,” Tetrahedron Letters, vol. 43, no. 16, pp. 2889–2890, 2002. View at Publisher · View at Google Scholar · View at Scopus
  297. B. A. Halkier and J. Gershenzon, “Biology and biochemistry of glucosinolates,” Annual Review of Plant Biology, vol. 57, pp. 303–333, 2006. View at Publisher · View at Google Scholar · View at Scopus
  298. H. Yuasa, M. M. Palcic, and O. Hindsgaul, “Synthesis of the carbocyclic analog of uridine 5′-(α-D-galactopyranosyl diphosphate) (UDP-gal) as an inhibitor of β(1→4)-galactosyltransferase,” Canadian Journal of Chemistry, vol. 73, no. 12, pp. 2190–2195, 1995. View at Publisher · View at Google Scholar · View at Scopus
  299. S. Cai, M. R. Stroud, S. Hakomori, and T. Toyokuni, “Synthesis of carbocyclic analogs of guanosine 5′-(β-l-fucopyranosyl diphosphate) (GDP-fucose) as potential inhibitors of fucosyltransferases,” The Journal of Organic Chemistry, vol. 57, no. 25, pp. 6693–6696, 1992. View at Publisher · View at Google Scholar · View at Scopus
  300. A. J. Norris, J. P. Whitelegge, M. J. Strouse, K. F. Faull, and T. Toyokuni, “Inhibition kinetics of carba- and C-fucosyl analogues of GDP-fucose against fucosyltransferase V: implication for the reaction mechanism,” Bioorganic and Medicinal Chemistry Letters, vol. 14, no. 3, pp. 571–573, 2004. View at Publisher · View at Google Scholar · View at Scopus
  301. L. Díaz and A. Delgado, “Medicinal chemistry of aminocyclitols,” Current Medicinal Chemistry, vol. 17, no. 22, pp. 2393–2418, 2010. View at Publisher · View at Google Scholar · View at Scopus
  302. S. Ogawa and M. Kanto, “Design and synthesis of 5a-carbaglycopyranosylamime glycosidase inhibitors,” Current Topics in Medicinal Chemistry, vol. 9, no. 1, pp. 58–75, 2009. View at Publisher · View at Google Scholar
  303. X. Chen, Y. Fan, Y. Zheng, and Y. Shen, “Properties and production of valienamine and its related analogues,” Chemical Reviews, vol. 103, no. 5, pp. 1955–1977, 2003. View at Publisher · View at Google Scholar · View at Scopus
  304. J.-F. Zhang, Y.-G. Zheng, and Y.-C. Shen, “Inhibitory effect of valienamine on the enzymatic activity of honeybee (Apis cerana Fabr.) α-glucosidase,” Pesticide Biochemistry and Physiology, vol. 87, no. 1, pp. 73–77, 2007. View at Publisher · View at Google Scholar · View at Scopus
  305. Y.-G. Zheng, X.-P. Shentu, and Y.-C. Shen, “Inhibition of porcine small intestinal sucrase by valienamine,” Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 20, no. 1, pp. 49–53, 2005. View at Publisher · View at Google Scholar · View at Scopus
  306. Y.-P. Xue, L.-Q. Jin, Z.-Q. Liu, J.-F. Zhang, and Y.-G. Zheng, “Purification and characterization of β-glucosidase from Reticulitermes flaviceps and its inhibition by valienamine and validamine,” African Journal of Biotechnology, vol. 7, no. 24, pp. 4595–4601, 2008. View at Google Scholar · View at Scopus
  307. Y. Zheng, X. Shentu, and Y. Shen, “Inhibition of porcine small intestinal sucrase by validamine,” Chinese Journal of Chemical Engineering, vol. 13, no. 3, pp. 429–432, 2005. View at Google Scholar · View at Scopus
  308. S. Ogawa, M. Oya, T. Toyokuni, N. Chida, and T. Suami, “Pseudo-sugars. VIII. Synthesis of DL-1-epivalidamine and related compounds,” Bulletin of the Chemical Society of Japan, vol. 56, no. 5, pp. 1441–1445, 1983. View at Publisher · View at Google Scholar · View at Scopus
  309. S. Ogawa, M. Suzuki, and T. Tonegawa, “New synthesis of Penta-N,O-acetyl-dl-validamine and pseudo-2-amino-2-deoxy-α-dl-mannopyranose, and their uronate analogs,” Bulletin of the Chemical Society of Japan, vol. 61, no. 5, pp. 1824–1826, 1988. View at Publisher · View at Google Scholar
  310. Y. Kameda, K. Kawashima, M. Takeuchi, K. Ikeda, N. Asano, and K. Matsui, “Preparation and biological activity of manno- and galacto-validamines, new 5a-carba-glycosylamines as α-glycosidase inhibitors,” Carbohydrate Research, vol. 300, no. 3, pp. 259–264, 1997. View at Publisher · View at Google Scholar · View at Scopus
  311. Y. Kameda, N. Asano, M. Yoshikawa et al., “Valiolamine, a new α-glucosidase inhibiting aminocyclitol. produced by Streptomyces hygroscopicus,” Journal of Antibiotics, vol. 37, no. 11, pp. 1301–1307, 1984. View at Publisher · View at Google Scholar · View at Scopus
  312. S. Horii, H. Fukase, T. Matsuo, Y. Kameda, N. Asano, and K. Matsui, “Synthesis and α-d-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents,” Journal of Medicinal Chemistry, vol. 29, no. 6, pp. 1038–1046, 1986. View at Publisher · View at Google Scholar · View at Scopus
  313. X. Chen, Y. Zheng, and Y. Shen, “Voglibose (Basen®, AO-128), one of the most important α-glucosidase inhibitors,” Current Medicinal Chemistry, vol. 13, no. 1, pp. 109–116, 2006. View at Publisher · View at Google Scholar
  314. A. S. Dabhi, N. R. Bhatt, and M. J. Shah, “Voglibose: an alpha glucosidase inhibitor,” Journal of Clinical and Diagnostic Research, vol. 7, no. 12, pp. 3023–3027, 2013. View at Publisher · View at Google Scholar · View at Scopus
  315. H. Konya, T. Katsuno, T. Tsunoda et al., “Effects of combination therapy with mitiglinide and voglibose on postprandial plasma glucose in patients with type 2 diabetes mellitus,” Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy, vol. 6, pp. 317–325, 2013. View at Publisher · View at Google Scholar · View at Scopus
  316. V. L. Campo, V. Aragão-Leoneti, and I. Carvalho, “Glycosidases and diabetes: metabolic changes, mode of action and therapeutic perspectives,” Carbohydrate Chemistry, vol. 39, pp. 181–203, 2013. View at Publisher · View at Google Scholar · View at Scopus
  317. G. Derosa and P. Maffioli, “α-Glucosidase inhibitors and their use in clinical practice,” Archives of Medical Science, vol. 8, no. 5, pp. 899–906, 2012. View at Publisher · View at Google Scholar · View at Scopus
  318. B.-H. Bin, J. Seo, S. H. Yang et al., “Novel inhibitory effect of the antidiabetic drug voglibose on melanogenesis,” Experimental Dermatology, vol. 22, no. 8, pp. 541–546, 2013. View at Publisher · View at Google Scholar · View at Scopus
  319. O. Lockhoff, “Glycolipids as immunomodulators: syntheses and properties,” Angewandte Chemie—International Edition in English, vol. 30, no. 12, pp. 1611–1620, 1991. View at Publisher · View at Google Scholar · View at Scopus
  320. H. Tsunoda, S.-I. Sasaki, T. Furuya, and S. Ogawa, “Pseudosugars, 36: synthesis of methyl 5′-carbamaltoses linked by imino, ether and sulfide bridges and unsaturated derivatives thereof,” Liebigs Annales, no. 2, pp. 159–165, 1996. View at Google Scholar · View at Scopus
  321. C. Ramstadius, O. Hekmat, L. Eriksson, H. Stålbrand, and I. Cumpstey, “β-Mannosidase and β-hexosaminidase inhibitors: synthesis of 1,2-bis-epi-valienamine and 1-epi-2-acetamido-2-deoxy-valienamine from d-mannose,” Tetrahedron Asymmetry, vol. 20, no. 6–8, pp. 795–807, 2009. View at Publisher · View at Google Scholar · View at Scopus
  322. A. Scaffidi, K. A. Stubbs, R. J. Dennis et al., “A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of β-N-acetylglucosaminidases,” Organic and Biomolecular Chemistry, vol. 5, no. 18, pp. 3013–3019, 2007. View at Publisher · View at Google Scholar · View at Scopus
  323. Y. Z. Frohwein and S. Gatt, “Isolation of β-N-acetylhexosaminidase, β-N-acetylglucosaminidase, and β-N-acetylgalactosaminidase from calf brain,” Biochemistry, vol. 6, no. 9, pp. 2775–2782, 1967. View at Publisher · View at Google Scholar · View at Scopus
  324. S. C. Li and Y. T. Li, “Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of beta-N-acetylhexosaminidase,” The Journal of Biological Chemistry, vol. 245, no. 19, pp. 5153–5160, 1970. View at Google Scholar · View at Scopus
  325. T. Liu, L. Chen, Q. Ma, X. Shen, and Q. Yang, “Structural insights into chitinolytic enzymes and inhibition mechanisms of selective inhibitors,” Current Pharmaceutical Design, vol. 20, no. 5, pp. 754–770, 2014. View at Publisher · View at Google Scholar · View at Scopus
  326. H. Tsunoda and S. Ogawa, “Pseudosugars, 33. Synthesis of some 5a-carbaglycosylamides, glycolipid analogs of biological interests,” Liebigs Annalen der Chemie, no. 2, pp. 103–107, 1994. View at Publisher · View at Google Scholar
  327. H. Tsunoda, J.-I. Inokuchi, K. Yamagishi, and S. Ogawa, “Pseudosugars, 35. Synthesis of glycosylceramide analogs composed of imino-linked unsaturated 5a-carbaglycosyl residues: potent and specific gluco- and galactocerebrosidase inhibitors,” Liebigs Annalen, no. 2, pp. 279–284, 1995. View at Publisher · View at Google Scholar
  328. S. Ogawa, M. Ashiuraa, C. Uchida et al., “Synthesis of potent β-D-glucocerebrosidase inhibitors: N-alkyl-β-valienamines,” Bioorganic and Medicinal Chemistry Letters, vol. 6, no. 8, pp. 929–932, 1996. View at Publisher · View at Google Scholar · View at Scopus
  329. S. Ogawa, T. Mito, E. Taiji, M. Jimbo, K. Yamagishi, and J.-I. Inokuchi, “Synthesis and biological evaluation of four stereoisomers of PDMP-analogue, N-(2-decylamino-3-hydroxy-3-phenylprop- 1-yl)-β-valienamine, and related compounds,” Bioorganic and Medicinal Chemistry Letters, vol. 7, no. 14, pp. 1915–1920, 1997. View at Publisher · View at Google Scholar · View at Scopus
  330. S. Ogawa, Y. Kobayashi, K. Kabayama, M. Jimbo, and J.-I. Inokuchi, “Chemical modification of β-glucocerebrosidase inhibitor N-octyl-β-valienamine: synthesis and biological evaluation of N-alkanoyl and N-alkyl derivatives,” Bioorganic and Medicinal Chemistry, vol. 6, no. 10, pp. 1955–1962, 1998. View at Publisher · View at Google Scholar · View at Scopus
  331. S. Horii, H. Fukase, T. Matsuo, Y. Kameda, N. Asano, and K. Matsui, “Synthesis and α-D-glucosidase inhibitory activity of N-substituted valiolamine derivatives as potential oral antidiabetic agents,” Journal of Medicinal Chemistry, vol. 29, no. 6, pp. 1038–1046, 1986. View at Publisher · View at Google Scholar · View at Scopus
  332. Y. Kameda, N. Asano, M. Yoshikawa, K. Matsui, S. Horii, and H. Fukase, “N-substituted valienamines, α-glucosidase inhibitors,” Journal of Antibiotics, vol. 35, no. 11, pp. 1624–1626, 1982. View at Publisher · View at Google Scholar · View at Scopus
  333. R. Łysek, C. Schütz, S. Favre et al., “Search for &-glucosidase inhibitors: new N-substituted valienamine and conduramine F-1 derivatives,” Bioorganic and Medicinal Chemistry, vol. 14, no. 18, pp. 6255–6282, 2006. View at Publisher · View at Google Scholar · View at Scopus
  334. P. Kapferer, V. Birault, J.-F. Poisson, and A. Vasella, “Synthesis and evaluation as glycosidase inhibitors of carbasugar-derived spirodiaziridines, spirodiazirines, and spiroaziridines,” Helvetica Chimica Acta, vol. 86, no. 6, pp. 2210–2227, 2003. View at Publisher · View at Google Scholar · View at Scopus
  335. Y. Wang and A. J. Bennet, “A potent bicyclic inhibitor of a family 27 α-galactosidase,” Organic and Biomolecular Chemistry, vol. 5, no. 11, pp. 1731–1738, 2007. View at Publisher · View at Google Scholar · View at Scopus
  336. Y. Suzuki, S. Ogawa, and Y. Sakakibara, “Chaperone therapy for neuronopathic lysosomal diseases: competitive inhibitors as chemical chaperones for enhancement of mutant enzyme activities,” Perspectives in Medicinal Chemistry, vol. 2009, no. 3, pp. 7–19, 2009. View at Google Scholar · View at Scopus
  337. Y. Suzuki, “Chemical chaperone therapy for GM1-gangliosidosis,” Cellular and Molecular Life Sciences, vol. 65, no. 3, pp. 351–353, 2008. View at Publisher · View at Google Scholar · View at Scopus
  338. Y. Suzuki, “β-Galactosidase deficiency: an approach to chaperone therapy,” Journal of Inherited Metabolic Disease, vol. 29, no. 2-3, pp. 471–476, 2006. View at Publisher · View at Google Scholar · View at Scopus
  339. J. Matsuda, O. Suzuki, A. Oshima et al., “Chemical chaperone therapy for brain pathology in G M1-gangliosidosis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 26, pp. 15912–15917, 2003. View at Publisher · View at Google Scholar · View at Scopus
  340. H. Lin, Y. Sugimoto, Y. Ohsaki et al., “N-Octyl-β-valienamine up-regulates activity of F213I mutant β-glucosidase in cultured cells: a potential chemical chaperone therapy for Gaucher disease,” Biochimica et Biophysica Acta—Molecular Basis of Disease, vol. 1689, no. 3, pp. 219–228, 2004. View at Publisher · View at Google Scholar · View at Scopus
  341. M. A. Hossain, K. Higaki, S. Saito et al., “Chaperone therapy for Krabbe disease: potential for late-onset GALC mutations,” Journal of Human Genetics, vol. 60, no. 9, pp. 539–545, 2015. View at Publisher · View at Google Scholar · View at Scopus
  342. S. Kuno, K. Higaki, A. Takahashi, E. Nanba, and S. Ogawa, “Potent chemical chaperone compounds for GM1-gangliosidosis: N-substituted (+)-conduramine F-4 derivatives,” MedChemComm, vol. 6, no. 2, pp. 306–310, 2015. View at Publisher · View at Google Scholar · View at Scopus
  343. Y. Suzuki, S. Ichinomiya, M. Kurosawa et al., “Therapeutic chaperone effect of N-Octyl 4-Epi-β-valienamine on murine GM1-gangliosidosis,” Molecular Genetics and Metabolism, vol. 106, no. 1, pp. 92–98, 2012. View at Publisher · View at Google Scholar · View at Scopus
  344. S. Kuno, A. Takahashi, and S. Ogawa, “Transformation of quercitols into 4-methylenecyclohex-5-ene-1,2,3-triol derivatives, precursors for the chemical chaperones N-octyl-4-epi-β- valienamine (NOEV) and N-octyl-β-valienamine (NOV),” Bioorganic and Medicinal Chemistry Letters, vol. 21, no. 23, pp. 7189–7192, 2011. View at Publisher · View at Google Scholar · View at Scopus
  345. Z. Luan, L. Li, H. Ninomiya et al., “The pharmacological chaperone effect of N-octyl-β-valienamine on human mutant acid β-glucosidases,” Blood Cells, Molecules, and Diseases, vol. 44, no. 1, pp. 48–54, 2010. View at Publisher · View at Google Scholar · View at Scopus
  346. Y. Suzuki, S. Ichinomiya, M. Kurosawa et al., “Chaperone therapy for neuronopathic lysosomal diseases: competitive inhibitors as chemical chaperones for enhancement of mutant enzyme activities,” Perspectives in Medicinal Chemistry, vol. 3, pp. 7–19, 2009. View at Google Scholar
  347. K. Lei, H. Ninomiya, M. Suzuki et al., “Enzyme enhancement activity of N-octyl-β-valienamine on β-glucosidase mutants associated with Gaucher disease,” Biochimica et Biophysica Acta—Molecular Basis of Disease, vol. 1772, no. 5, pp. 587–596, 2007. View at Publisher · View at Google Scholar · View at Scopus
  348. M. A. Hossain, K. Higaki, M. Shinpo et al., “Chemical chaperone treatment for galactosialidosis: effect of NOEV on β-galactosidase activities in fibroblasts,” Brain and Development, vol. 38, no. 2, pp. 175–180, 2016. View at Publisher · View at Google Scholar · View at Scopus
  349. H. Suzuki, U. Ohto, K. Higaki et al., “Structural basis of pharmacological chaperoning for human β-galactosidase,” The Journal of Biological Chemistry, vol. 289, no. 21, pp. 14560–14568, 2014. View at Publisher · View at Google Scholar · View at Scopus
  350. A. Takamura, K. Higaki, H. Ninomiya et al., “Lysosomal accumulation of Trk protein in brain of GM1—gangliosidosis mouse and its restoration by chemical chaperone,” Journal of Neurochemistry, vol. 118, no. 3, pp. 399–406, 2011. View at Publisher · View at Google Scholar · View at Scopus
  351. Z. Luan, H. Ninomiya, K. Ohno et al., “The effect of N-octyl-β-valienamine on β-glucosidase activity in tissues of normal mice,” Brain and Development, vol. 32, no. 10, pp. 805–809, 2010. View at Publisher · View at Google Scholar · View at Scopus
  352. G. Parenti, G. Andria, and K. J. Valenzano, “Pharmacological chaperone therapy: preclinical development, clinical translation, and prospects for the treatment of lysosomal storage disorders,” Molecular Therapy, vol. 23, no. 7, pp. 1138–1148, 2015. View at Publisher · View at Google Scholar · View at Scopus
  353. G. Parenti, M. Moracci, S. Fecarotta, and G. Andria, “Pharmacological chaperone therapy for lysosomal storage diseases,” Future Medicinal Chemistry, vol. 6, no. 9, pp. 1031–1045, 2014. View at Publisher · View at Google Scholar · View at Scopus
  354. B. Winchester, A. Vellodi, and E. Young, “The molecular basis of lysosomal storage diseases and their treatment,” Biochemical Society Transactions, vol. 28, no. 2, pp. 150–154, 2000. View at Publisher · View at Google Scholar · View at Scopus
  355. S. Ogawa, R. Sekura, A. Maruyama, H. Yuasa, and H. Hashimoto, “Synthesis and glycosidase inhibitory activity of 5a-carba-α-dl-fucopyranosylamine and -galactopyranosylamine,” European Journal of Organic Chemistry, vol. 2000, no. 11, pp. 2089–2093, 2000. View at Publisher · View at Google Scholar
  356. S. Ogawa, A. Maruyama, T. Odagiri, H. Yuasa, and H. Hashimoto, “Synthesis and biological evaluation of α-L-fucosidase inhibitors: 5a-carba-α-L-fucopyranosylamine and related compounds,” European Journal of Organic Chemistry, no. 5, pp. 967–974, 2001. View at Google Scholar · View at Scopus
  357. S. Ogawa, M. Watanabe, A. Maruyama, and S. Hisamatsu, “Synthesis of an α-fucosidase inhibitor, 5a-carba-β-L-fucopyranosylamine, and fucose-type α- and β-DL-valienamine unsaturated derivatives,” Bioorganic and Medicinal Chemistry Letters, vol. 12, no. 5, pp. 749–752, 2002. View at Publisher · View at Google Scholar · View at Scopus
  358. R. J. Bernacki, M. J. Niedbala, and W. Korytnyk, “Glycosidases in cancer and invasion,” Cancer and Metastasis Review, vol. 4, no. 1, pp. 81–101, 1985. View at Publisher · View at Google Scholar · View at Scopus
  359. S. Ogawa, M. Mori, G. Takeuchi, F. Doi, M. Watanabe, and Y. Sakata, “Convenient synthesis and evaluation of enzyme inhibitory activity of several N-alkyl-, N-phenylalkyl, and cyclic isourea derivatives of 5a-Carba-α-DL-fucopyranosylamine,” Bioorganic and Medicinal Chemistry Letters, vol. 12, no. 20, pp. 2811–2814, 2002. View at Publisher · View at Google Scholar · View at Scopus
  360. S. Ogawa, S. Fujieda, Y. Sakata, M. Ishizaki, S. Hisamatsu, and K. Okazaki, “Synthesis and glycosidase inhibitory activity of some N-substituted 6-deoxy-5a-carba-β-dl- and L-galactopyranosylamines,” Bioorganic and Medicinal Chemistry Letters, vol. 13, no. 20, pp. 3461–3463, 2003. View at Publisher · View at Google Scholar · View at Scopus
  361. J. W. Gavin, S. T. Jon, and E. J. Toone, “Natural product glycosyltransferases: properties and applications,” Advances in Enzymology and Related Areas of Molecular Biology, vol. 76, pp. 55–119, 2009. View at Google Scholar · View at Scopus
  362. Y. Kajihara, H. Hashimoto, and S. Ogawa, “Galactosyl transfer ability of β-(1→4)-galactosyltransferase toward 5a-carba-sugars,” Carbohydrate Research, vol. 323, no. 1–4, pp. 44–48, 1999. View at Publisher · View at Google Scholar · View at Scopus
  363. H. Qian, B. Hu, Z. Wang, X. Xu, and T. Hong, “Effects of validamycin on some enzymatic activities in soil,” Environmental Monitoring and Assessment, vol. 125, no. 1–3, pp. 1–8, 2007. View at Publisher · View at Google Scholar · View at Scopus
  364. R. Ishikawa, K. Shirouzu, H. Nakashita, T. Teraoka, and T. Arie, “Control efficacy of validamycin A against Fusarium wilt correlated with the severity of phytotoxic necrosis formed on tomato tissues,” Journal of Pesticide Science, vol. 32, no. 2, pp. 83–88, 2007. View at Publisher · View at Google Scholar · View at Scopus
  365. B. M. Naik, J. Priya, K. U. Solanky, L. Mahatma, B. P. Mehta, and A. N. Sabalpara, “Evaluation of newer fungicides for the management of foliar pathogens of banana,” Pestology, vol. 34, no. 10, pp. 40–43, 2010. View at Google Scholar · View at Scopus
  366. Y. H. Lee, C. W. Choi, S. H. Kim et al., “Chemical pesticides and plant essential oils for disease control of tomato bacterial wilt,” Plant Pathology Journal, vol. 28, no. 1, pp. 32–39, 2012. View at Publisher · View at Google Scholar · View at Scopus
  367. J. P. Guirao-Abad, R. Sánchez-Fresneda, E. Valentín, M. Martínez-Esparza, and J.-C. Argüelles, “Analysis of validamycin as a potential antifungal compound against Candida albicans,” International Microbiology, vol. 16, no. 4, pp. 217–225, 2013. View at Publisher · View at Google Scholar · View at Scopus
  368. S. Nwaka and H. Holzer, “Molecular biology of trehalose and the trehalases in the yeast Saccharomyces cerevisiae,” Progress in nucleic acid research and molecular biology, vol. 58, pp. 197–237, 1998. View at Google Scholar · View at Scopus
  369. A. Barraza and F. Sánchez, “Trehalases: a neglected carbon metabolism regulator?” Plant Signaling & Behavior, vol. 8, no. 7, Article ID e24778, 2013. View at Publisher · View at Google Scholar · View at Scopus
  370. J. Müller, T. Boller, and A. Wiemken, “Trehalose and trehalase in plants: recent developments,” Plant Science, vol. 112, no. 1, pp. 1–9, 1995. View at Publisher · View at Google Scholar · View at Scopus
  371. N. Tatun, O. Wangsantitham, J. Tungjitwitayakul, and S. Sakurai, “Trehalase activity in fungus-growing termite, Odontotermes feae (Isoptera: Termitideae) and inhibitory effect ofvalidamycin,” Journal of Economic Entomology, vol. 107, no. 3, pp. 1224–1232, 2014. View at Publisher · View at Google Scholar · View at Scopus
  372. S. Lenka, G. Bhaktavatsalam, and B. Medhi, “Fungicidal control of sheath blight of rice,” Journal of Plant Protection and Environment, vol. 7, pp. 53–55, 2010. View at Google Scholar
  373. V. Bhuvaneswari and S. K. Raju, “Efficacy of new fungicide of strobilurin group against rice sheath blight caused by Rhizoctonia solani,” Journal of Mycology and Plant Pathology, vol. 43, pp. 447–451, 2013. View at Google Scholar
  374. O. Wakae and K. Matsuura, “Characteristics of validamycin as a fungicide for Rhizoctonia disease control. Review,” Journal of Plant Protection Research, vol. 8, pp. 81–92, 1975. View at Google Scholar
  375. J. Serneels, H. Tournu, and P. Van Dijck, “Tight control of trehalose content is required for efficient heat-induced cell elongation in Candida albicans,” The Journal of Biological Chemistry, vol. 287, no. 44, pp. 36873–36882, 2012. View at Publisher · View at Google Scholar · View at Scopus
  376. Z.-J. Wang, S. Ji, Y.-X. Si et al., “The effect of validamycin A on tyrosinase: inhibition kinetics and computational simulation,” International Journal of Biological Macromolecules, vol. 55, pp. 15–23, 2013. View at Publisher · View at Google Scholar · View at Scopus
  377. Y. H. Lee, Y.-S. Cho, S. W. Lee, and J. K. Hong, “Chemical and biological controls of balloon flower stem rots caused by Rhizoctonia solani and Sclerotinia sclerotiorum,” Plant Pathology Journal, vol. 28, no. 2, pp. 156–163, 2012. View at Publisher · View at Google Scholar · View at Scopus
  378. H. Berga and N. T. Tamb, “Use of pesticides and attitude to pest management strategies among rice and rice-fish farmers in the mekong delta, Vietnam,” International Journal of Pest Management, vol. 58, no. 2, pp. 153–164, 2012. View at Publisher · View at Google Scholar · View at Scopus
  379. H. Li, H. Su, S. B. Kim et al., “Enhanced production of trehalose in Escherichia coli by homologous expression of otsBA in the presence of the trehalase inhibitor, validamycin A, at high osmolarity,” Journal of Bioscience and Bioengineering, vol. 113, no. 2, pp. 224–232, 2012. View at Publisher · View at Google Scholar · View at Scopus
  380. K. Qian, T. Shi, T. Tang, S. Zhang, X. Liu, and Y. Cao, “Preparation and characterization of nano-sized calcium carbonate as controlled release pesticide carrier for validamycin against Rhizoctonia solani,” Microchimica Acta, vol. 173, no. 1-2, pp. 51–57, 2011. View at Publisher · View at Google Scholar · View at Scopus
  381. M. Best, K. Koenig, K. McDonald, M. Schueller, A. Rogers, and R. A. Ferrieri, “Inhibition of trehalose breakdown increases new carbon partitioning into cellulosic biomass in Nicotiana tabacum,” Carbohydrate Research, vol. 346, no. 5, pp. 595–601, 2011. View at Publisher · View at Google Scholar · View at Scopus
  382. A. Biswas and M. K. Bag, “Strobilurins in management of sheath blight disease of rice: a review,” Pestology, vol. 34, no. 4, pp. 23–26, 2010. View at Google Scholar · View at Scopus
  383. L.-Q. Jin and Y.-G. Zheng, “Inhibitory effects of validamycin compounds on the termites trehalase,” Pesticide Biochemistry and Physiology, vol. 95, no. 1, pp. 28–32, 2009. View at Publisher · View at Google Scholar · View at Scopus
  384. M. López, N. A. Tejera, and C. Lluch, “Validamycin A improves the response of Medicago truncatula plants to salt stress by inducing trehalose accumulation in the root nodules,” Journal of Plant Physiology, vol. 166, no. 11, pp. 1218–1222, 2009. View at Publisher · View at Google Scholar · View at Scopus
  385. R. P. Gibson, T. M. Gloster, S. Roberts et al., “Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors,” Angewandte Chemie—International Edition, vol. 46, no. 22, pp. 4115–4119, 2007. View at Publisher · View at Google Scholar · View at Scopus
  386. M. J. Madigan and J. Martinko, Eds., Brock Biology of Microorganisms, Prentice Hall, 11th edition, 2005.
  387. T. Nioh and S. Mizushima, “Effect of validamycin on the growth and morphology of Pellicularia sasakii,” Journal of General and Applied Microbiology, vol. 20, no. 6, pp. 373–383, 1974. View at Publisher · View at Google Scholar · View at Scopus
  388. M. Uyeda, A. Ikeda, T. Machimoto, and M. Shibata, “Effect of validamycin on production of some enzymes in Rhizoctonia solani,” Agricultural and Biological Chemistry, vol. 49, no. 12, pp. 3485–3491, 1985. View at Google Scholar · View at Scopus
  389. Y. Kido, T. Nagasato, and K. Ono, “Change in a cell-wall component of Rhizoctonia solani inhibited by validamycin,” Agricultural and Biological Chemistry, vol. 50, no. 6, pp. 1519–1525, 1986. View at Google Scholar · View at Scopus
  390. M. Uyeda, A. Ikeda, T. Ogata, and M. Shibata, “Effect of validamycin on β-D-glucan-degrading enzymes from Rhizoctonia solani,” Agricultural and Biological Chemistry, vol. 50, no. 7, pp. 1885–1886, 1986. View at Google Scholar · View at Scopus
  391. Y. Kameda, N. Asano, T. Yamaguchi, and K. Matsui, “Validoxylamines as trehalase inhibitors,” Journal of Antibiotics, vol. 40, no. 4, pp. 563–565, 1987. View at Publisher · View at Google Scholar · View at Scopus
  392. N. Asano, M. Takeuchi, Y. Kameda, K. Matsui, and Y. Kono, “Trehalase inhibitors, validoxylamine A and related compounds as insecticides,” Journal of Antibiotics, vol. 43, no. 6, pp. 722–726, 1990. View at Publisher · View at Google Scholar · View at Scopus
  393. R. Shigemoto, T. Okuno, and K. Matsuura, “Effects of validamycin A on the growth of and trehalose content in mycelia of Rhizoctonia solani incubated in a medium containing several sugars as the sole carbohydrate,” Annals of the Phytopathological Society of Japan, vol. 58, pp. 685–690, 1992. View at Google Scholar
  394. N. Asano, T. Yamaguchi, Y. Kameda, and K. Matsui, “Effect of validamycins on glycohydrolases of Rhizoctonia solani,” Journal of Antibiotics, vol. 40, no. 4, pp. 526–532, 1987. View at Publisher · View at Google Scholar · View at Scopus
  395. S. Ogawa, K. Sato, and Y. Miyamoto, “Synthesis and trehalase-inhibitory activity of an imino-linked dicarba-α,α-trehalose and analogues thereof,” Journal of the Chemical Society, Perkin Transactions 1, no. 6, pp. 691–696, 1993. View at Google Scholar · View at Scopus
  396. S. Ogawa, K. Nishi, and Y. Shibata, “Synthesis of a carba-sugar analog of trehalosamine, [(1S)-(1,2, 4 3,5)-2-amino-3,4-dihydroxy-5-hydroxymethyl-1-cyclohexyl] α-d-glucopyranoside, and a revised synthesis of its β anomer,” Carbohydrate Research, vol. 206, no. 2, pp. 352–360, 1990. View at Publisher · View at Google Scholar · View at Scopus
  397. S. Ogawa and Y. Shibata, “Synthesis of biologically active pseudo-trehalosamine: [(1S)-(1,2,4/3,5)-2,3,4-trihydroxy-5-hydroxymethyl-1-cyclohexyl] 2-amino-2-deoxy-α-d-glucopyranoside,” Carbohydrate Research, vol. 176, no. 2, pp. 309–315, 1988. View at Publisher · View at Google Scholar · View at Scopus
  398. K.-I. Fukuhara, H. Murai, and S. Murao, “Isolation and structure-activity relationship of some amylostatins (F-1b fraction) produced by streptomyces diastaticus subsp. amylostaticus,” Agricultural and Biological Chemistry, vol. 46, no. 7, pp. 1941–1945, 1982. View at Publisher · View at Google Scholar
  399. S. Namiki, K. Kangouri, T. Nagate et al., “Studies on the α-glucoside hydrolase inhibitor, adiposin. IV. Effect of adiposin on intestinal digestion of carbohydrates in experimental animals,” Journal of Antibiotics, vol. 35, no. 9, pp. 1167–1173, 1982. View at Publisher · View at Google Scholar · View at Scopus
  400. S. Omoto, J. Itoh, T. Shomura et al., “Oligostatins, new antibiotics with amylase inhibitory activity. I. Production, isolation and characterization,” Journal of Antibiotics, vol. 34, no. 11, pp. 1424–1428, 1981. View at Publisher · View at Google Scholar · View at Scopus
  401. S. Ogawa, Y. Shibata, Y. Kosuge, K. Yasuda, T. Mizukoshi, and C. Uchida, “Synthesis of potent α-glucosidase inhibitors: Methyl acarviosin analogue composed of 1,6-anhydro-β-D-glucopyranose residue,” Journal of the Chemical Society, Chemical Communications, no. 20, pp. 1387–1388, 1990. View at Google Scholar · View at Scopus
  402. Y. Shibata, Y. Kosuge, T. Mizukoshi, and S. Ogawa, “Chemical modification of the sugar part of methyl acarviosin: synthesis and inhibitory activities of nine analogues,” Carbohydrate Research, vol. 228, no. 2, pp. 377–398, 1992. View at Publisher · View at Google Scholar · View at Scopus
  403. S. Ogawa and D. Aso, “Chemical modification of the sugar moiety of methyl acarviosin: synthesis and inhibitory activity of eight analogues containing a 1,6-anhydro bridge,” Carbohydrate Research, vol. 250, no. 1, pp. 177–184, 1993. View at Publisher · View at Google Scholar · View at Scopus
  404. S. Ogawa, S. Ogawa, and H. Tsunoda, “Chemical synthesis of glycosylamide and cerebroside analogs composed of carba sugars,” Methods in Enzymology, vol. 247, pp. 136–143, 1994. View at Publisher · View at Google Scholar · View at Scopus
  405. S. Ogawa, S.-I. Sasaki, and H. Tsunoda, “Synthesis of carbocyclic analogues of the mannosyl trisaccharide: ether- and imino-linked methyl 3,6-bis(5a-carba-α-d-mannopyranosyl)-3,6-dideoxy-α-d-mannopyranosides,” Carbohydrate Research, vol. 274, pp. 183–196, 1995. View at Publisher · View at Google Scholar · View at Scopus
  406. S. Ogawa, T. Furuya, H. Tsunoda, O. Hindsgaul, K. Stangier, and M. M. Palcic, “Synthesis of β-d-GlcpNAc-(1 → 2)-5a-carba-α-d-Manp-(1 → 6)-β-d-Glcp-O(CH2)7CH3: a reactive acceptor analog for N-acetylglucosaminyltransferase-V,” Carbohydrate Research, vol. 271, no. 2, pp. 197–205, 1995. View at Publisher · View at Google Scholar · View at Scopus
  407. S. I. Hakomori, “Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens,” Advances in Cancer Research, vol. 52, pp. 257–331, 1989. View at Publisher · View at Google Scholar · View at Scopus
  408. H. Schachter, “Molecular cloning of glycosyltranferase genes,” in Molecular Glycobiology, M. Fukuda and O. Hindsgaul, Eds., pp. 86–162, IRL Press, New York, NY, USA, 1994. View at Google Scholar
  409. J. P. Prieels, D. Monnom, M. Dolmans, T. A. Beyer, and R. L. Hill, “Co-purification of the Lewis blood group N-acetylglucosaminide alpha 1 goes to 4 fucosyltransferase and an N-acetylglucosaminide alpha 1 goes to 3 fucosyltransferase from human milk,” The Journal of Biological Chemistry, vol. 256, pp. 10456–10463, 1981. View at Google Scholar
  410. B. A. Macher, E. H. Holmes, S. J. Swiedler, C. L. M. Stults, and C. A. Srnka, “Human α1–3 fucosyltransferases,” Glycobiology, vol. 1, no. 6, pp. 577–584, 1991. View at Publisher · View at Google Scholar · View at Scopus
  411. T. de Vries, R. M. A. Knegtel, E. H. Holmes, and B. A. Macher, “Fucosyltransferases: structure/function studies,” Glycobiology, vol. 11, no. 10, pp. 119R–128R, 2001. View at Google Scholar · View at Scopus
  412. D. J. Becker and J. B. Lowe, “Fucose: biosynthesis and biological function in mammals,” Glycobiology, vol. 13, no. 7, pp. 41R–53R, 2003. View at Publisher · View at Google Scholar · View at Scopus
  413. S. Ogawa, N. Matsunaga, and M. M. Palcic, “Synthesis of biological interest: ether linked octyl 5a-carba-β-lactosaminide and related compounds,” Carbohydrate letters, vol. 2, pp. 299–306, 1997. View at Google Scholar
  414. S. Ogawa, N. Matsunaga, H. Li, and M. M. Palcic, “Synthesis of ether- and imino-linked octyl N-Acetyl-5a′-carba-β-lactosaminides and -isolactosaminides: acceptor substrates for α-(13/4)-fucosyltransferase, and enzymatic synthesis of 5a′-carbatrisaccharides,” European Journal of Organic Chemistry, no. 3, pp. 631–642, 1999. View at Google Scholar
  415. S. Ogawa, K. Gamou, Y. Kugimiya, Y. Senba, A. Lu, and M. M. Palcic, “Synthesis of octyl N-acetyl-5a-carba-β-lactosaminide and-isolactosaminide: acceptor substrates for α1,3-fucosyltransferase V and α2,3-(N) sialyltransferase,” Carbohydrate Letters, vol. 3, no. 6, pp. 451–456, 2000. View at Google Scholar · View at Scopus
  416. K. Okazaki, S. Nishigaki, F. Ishizuka, Y. Kajihara, and S. Ogawa, “Potent and specific sialyltransferase inhibitors: imino-linked 5a′-carbadisaccharides,” Organic and Biomolecular Chemistry, vol. 1, no. 13, pp. 2229–2230, 2003. View at Publisher · View at Google Scholar · View at Scopus
  417. N. Kawamura, N. Kinoshita, R. Sawa et al., “Pyralomicins, novel antibiotics from Microtetraspora spiralis. I. Taxonomy and production,” Journal of Antibiotics, vol. 49, no. 7, pp. 706–709, 1996. View at Publisher · View at Google Scholar · View at Scopus