- About this Journal ·
- Abstracting and Indexing ·
- Advance Access ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Journal of Amino Acids
Volume 2011 (2011), Article ID 352538, 11 pages
The Catalytic Machinery of a Key Enzyme in Amino Acid Biosynthesis
1Department of Chemistry, University of Toledo, Toledo, OH 43606, USA
2Structural Biology Lab, Cold Spring Harbor Labs, Cold Spring Harbor, NY 11724, USA
3Rocky Mountain Labs, National Institutes of Health, Hamilton, MT 59840, USA
4Department of Pharmacology, Yale University, New Haven, CT 06520, USA
Received 2 October 2010; Accepted 7 November 2010
Academic Editor: Shandar Ahmad
Copyright © 2011 Ronald E. Viola et al. 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.
- C. L. Maree, R. S. Daum, S. Boyle-Vavra, K. Matayoshi, and L. G. Miller, “Community-associated methicillin-resistant Staphylococcus aureus isolates causing healthcare-associated infections,” Emerging Infectious Diseases, vol. 13, no. 2, pp. 236–242, 2007.
- N. S. Shah, A. Wright, G. H. Bai et al., “Worldwide emergence of extensively drug-resistant tuberculosis,” Emerging Infectious Diseases, vol. 13, no. 3, pp. 380–387, 2007.
- E. Almaas, Z. N. Oltvai, and A. L. Barabási, “The activity reaction core and plasticity of metabolic networks,” PLoS Computational Biology, vol. 1, no. 7, pp. 557–563, 2005.
- R. E. Viola, “The central enzymes of the aspartate family of amino acid biosynthesis,” Accounts of Chemical Research, vol. 34, no. 5, pp. 339–349, 2001.
- G. N. Cohen, “The common pathway to lysine, methionine, and threonine,” in Amino Acids: Biosynthesis and Genetic Regulation, K. M. Herrmann and R. L. Somerville, Eds., pp. 147–171, Addison-Wesley, Reading, Mass, USA, 1983.
- K. Ragkousi, P. Eichenberger, C. Van Ooij, and P. Setlow, “Identification of a new gene essential for germination of Bacillus subtilis spores with Ca-dipicolinate,” Journal of Bacteriology, vol. 185, no. 7, pp. 2315–2329, 2003.
- J. Van Heijenoort, “Recent advances in the formation of the bacterial peptidoglycan monomer unit,” Natural Product Reports, vol. 18, no. 5, pp. 503–519, 2001.
- G. J. Lyon and R. P. Novick, “Peptide signaling in Staphylococcus aureus and other Gram-positive bacteria,” Peptides, vol. 25, no. 9, pp. 1389–1403, 2004.
- X. Chen, S. Schauder, N. Potier et al., “Structural identification of a bacterial quorum-sensing signal containing boron,” Nature, vol. 415, no. 6871, pp. 545–549, 2002.
- C. Niu, K. M. Clemmer, R. A. Bonomo, and P. N. Rather, “Isolation and characterization of an autoinducer synthase from Acinetobacter baumannii,” Journal of Bacteriology, vol. 190, no. 9, pp. 3386–3392, 2008.
- J. E. Galan, K. Nakayama, and R. Curtiss, “Cloning and characterization of the asd gene of Salmonella typhimurium: use in stable maintenance of recombinant plasmids in Salmonella vaccine strains,” Gene, vol. 94, no. 1, pp. 29–35, 1990.
- A. Burkovski and R. Krämer, “Bacterial amino acid transport proteins: occurrence, functions, and significance for biotechnological applications,” Applied Microbiology and Biotechnology, vol. 58, no. 3, pp. 265–274, 2002.
- K. Gokulan, B. Rupp, M. S. Pavelka, W. R. Jacobs, and J. C. Sacchettini, “Crystal structure of Mycobacterium tuberculosis diaminopimelate decarboxylase, an essential enzyme in bacterial lysine biosynthesis,” Journal of Biological Chemistry, vol. 278, no. 20, pp. 18588–18596, 2003.
- A. Hadfield, G. Kryger, J. Ouyang, G. A. Petsko, D. Ringe, and R. Viola, “Structure of aspartate-β-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis,” Journal of Molecular Biology, vol. 289, no. 4, pp. 991–1002, 1999.
- A. Hadfield, C. Shammas, G. Kryger et al., “Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase,” Biochemistry, vol. 40, no. 48, pp. 14475–14483, 2001.
- J. Blanco, R. A. Moore, V. Kabaleeswaran, and R. E. Viola, “A structural basis for the mechanism of aspartate-β-semialdehyde dehydrogenase from Vibrio cholerae,” Protein Science, vol. 12, no. 1, pp. 27–33, 2003.
- J. Blanco, R. A. Moore, and R. E. Viola, “Capture of an intermediate in the catalytic cycle of L-aspartate-β -semialdehyde dehydrogenase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 22, pp. 12613–12617, 2003.
- C. R. Faehnle, J. Le Coq, X. Liu, and R. E. Viola, “Examination of key intermediates in the catalytic cycle of aspartate-β-semialdehyde dehydrogenase from a Gram-positive infectious bacteria,” Journal of Biological Chemistry, vol. 281, no. 41, pp. 31031–31040, 2006.
- C. R. Faehnle, J. F. Ohren, and R. E. Viola, “A new branch in the family: structure of aspartate-β-semialdehyde dehydrogenase from Methanococcus jannaschii,” Journal of Molecular Biology, vol. 353, no. 5, pp. 1055–1068, 2005.
- B. T. Arachea, X. Liu, A. G. Pavlovsky, and R. E. Viola, “Expansion of the aspartate β-semialdehyde dehydrogenase family: the first structure of a fungal ortholog,” Acta Crystallographica D, vol. 66, no. 2, pp. 205–212, 2010.
- W. E. Karsten and R. E. Viola, “Identification of an essential cysteine in the reaction catalyzed by aspartate-β-semialdehyde dehydrogenase from Escherichia coli,” Biochimica et Biophysica Acta, vol. 1121, no. 1-2, pp. 234–238, 1992.
- J. Blanco, R. A. Moore, C. R. Faehnle, and R. E. Vioła, “Critical catalytic functional groups in the mechanism of aspartate-beta;-semialdehyde dehydrogenase,” Acta Crystallographica D, vol. 60, no. 10, pp. 1808–1815, 2004.
- H. L. Segal and P. D. Boyer, “The role of sulfhydryl groups in the activity of D-glyceraldehyde 3-phosphate dehydrogenase,” The Journal of Biological Chemistry, vol. 204, no. 1, pp. 265–281, 1953.
- J. Ouyang and R. E. Viola, “Use of structural comparisons to select mutagenic targets in aspartate-β-semialdehyde dehydrogenase,” Biochemistry, vol. 34, no. 19, pp. 6394–6399, 1995.
- J. Blanco, R. A. Moore, C. R. Faehnle, D. M. Coe, and R. E. Viola, “The role of substrate-binding groups in the mechanism of aspartate-β-semialdehyde dehydrogenase,” Acta Crystallographica D, vol. 60, no. 8, pp. 1388–1395, 2004.
- T. Skarzński, P. C. E. Moody, and A. J. Wonacott, “Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution,” Journal of Molecular Biology, vol. 193, no. 1, pp. 171–187, 1987.
- M. M. Kish and R. E. Viola, “Oxyanion specificity of aspartate-β-semialdehyde dehydrogenase,” Inorganic Chemistry, vol. 38, no. 4, pp. 818–820, 1999.
- C. R. Faehnle, J. Blanco, and R. E. Viola, “Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-β-semialdehyde dehydrogenase,” Acta Crystallographica D, vol. 60, no. 12, pp. 2320–2324, 2004.
- S. T. Rao and M. G. Rossmann, “Comparison of super secondary structures in proteins,” Journal of Molecular Biology, vol. 76, no. 2, pp. 241–256, 1973.
- R. E. Viola, X. Liu, J. F. Ohren, and C. R. Faehnle, “The structure of a redundant enzyme: a second isoform of aspartate β-semialdehyde dehydrogenase in Vibrio cholerae,” Acta Crystallographica D, vol. 64, no. 3, pp. 321–330, 2008.
- J. F. Biellmann, P. Eid, C. Hirth, and H. Jornvall, “Aspartate-β-semialdehyde dehydrogenase from Escherichia coli. Affinity labeling with the substrate analogue L-2-amino-4-oxo-5-chloropentanoic acid: an example of half-site reactivity,” European Journal of Biochemistry, vol. 104, no. 1, pp. 59–64, 1980.
- J. F. Biellmann, P. Eid, and C. Hirth, “Affinity labeling of the Escherichia coli aspartate-β-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue,” European Journal of Biochemistry, vol. 104, no. 1, pp. 65–69, 1980.
- G. Gao, X. Liu, A. Pavlovsky, and R. E. Viola, “Identification of selective enzyme inhibitors by fragment library screening,” Journal of Biomolecular Screening, vol. 15, pp. 1042–1050, 2010.