- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Recently Accepted Articles ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 353270, 10 pages
Asymmetry of the Active Site Loop Conformation between Subunits of Glutamate-1-semialdehyde Aminomutase in Solution
1Dipartimento di Farmacia, Università di Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy
2Dipartimento di Neuroscienze, Università di Parma, Via Volturno 39, 43125 Parma, Italy
3Istituto Nazionale di Biostrutture e Biosistemi, Viale Medaglie d’Oro 305, 00136 Roma, Italy
4Dipartimento di Scienze Biochimiche “A. Rossi-Fanelli”, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Roma, Italy
Received 15 May 2013; Accepted 27 June 2013
Academic Editor: Barbara Cellini
Copyright © 2013 Barbara Campanini 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.
- P. M. Jordan and D. Shemin, δ-Aminolevulinic Acid Synthetase, in the Enzymes, Academic Press, New York, NY, USA, 1972.
- S. I. Beale and J. D. Weinstein, Biosynthesis of Haem and Chlorophylls, McGraw-Hill, New York, NY, USA, 1990.
- C. G. Kannangara, S. P. Gough, P. Bruyant, J. K. Hoober, A. Kahn, and D. von Wettstein, “tRNA(Glu) as a cofactor in delta-aminolevulinate biosynthesis: steps that regulate chlorophyll synthesis,” Trends in Biochemical Sciences, vol. 13, pp. 139–143, 1988.
- N. V. Grishin, M. A. Phillips, and E. J. Goldsmith, “Modeling of the spatial structure of eukaryotic ornithine decarboxylases,” Protein Science, vol. 4, pp. 1291–1304, 1995.
- R. Contestabile, T. Jenn, M. Akhtar, D. Gani, and R. A. John, “Reactions of glutamate 1-semialdehyde aminomutase with R- and S- enantiomers of a novel, mechanism-based inhibitor, 2,3-diaminopropyl sulfate,” Biochemistry, vol. 39, no. 11, pp. 3091–3096, 2000.
- M. A. Smith, C. G. Kannangara, B. Grimm, and D. Von Wettstein, “Characterization of glutamate-1-semialdehyde aminotransferase of Synechococcus. Steady-state kinetic analysis,” European Journal of Biochemistry, vol. 202, no. 3, pp. 749–757, 1991.
- M. A. Smith, B. Grimm, C. G. Kannangara, and D. Von Wettstein, “Spectral kinetics of glutamate-1-semialdehyde aminomutase of Synechococcus,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 21, pp. 9775–9779, 1991.
- C. E. Pugh, J. L. Harwood, and R. A. John, “Mechanism of glutamate semialdehyde aminotransferase: roles of diamino- and dioxo-intermediates in the synthesis of aminolevulinate,” Journal of Biological Chemistry, vol. 267, no. 3, pp. 1584–1588, 1992.
- P. Christen and D. E. Metzler, Transaminases, Wiley, New York, NY, USA, 1995.
- R. J. Tyacke, J. L. Harwood, and R. A. John, “Properties of the pyridoxaldimine form of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1-aminomutase) and analysis of its role as an intermediate in the formation of aminolaevulinate,” Biochemical Journal, vol. 293, part 3, pp. 697–701, 1993.
- B. Grimm, A. J. Smith, C. G. Kannangara, and M. Smith, “Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of Synechococcus: deletion of a tripeptide close to the NH2 terminus and internal amino acid substitution,” Journal of Biological Chemistry, vol. 266, no. 19, pp. 12495–12501, 1991.
- L. L. Ilag and D. Jahn, “Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R,” Biochemistry, vol. 31, no. 31, pp. 7143–7151, 1992.
- S. D'Aguanno, I. N. Gonzales, M. Simmaco, R. Contestabile, and R. A. John, “Stereochemistry of the reactions of glutamate-1-semialdehyde aminomutase with 4,5-diaminovalerate,” Journal of Biological Chemistry, vol. 278, no. 42, pp. 40521–40526, 2003.
- M. Hennig, B. Grimm, R. Contestabile, R. A. John, and J. N. Jansonius, “Crystal structure of glutamate-1-semialdehyde aminomutase: an α2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 10, pp. 4866–4871, 1997.
- J. Stetefeld, M. Jenny, and P. Burkhard, “Intersubunit signaling in glutamate-1-semialdehyde-aminomutase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 37, pp. 13688–13693, 2006.
- R. Contestabile, S. Angelaccio, R. Maytum, F. Bossa, and R. A. John, “The contribution of a conformationally mobile, active site loop to the reaction catalyzed by glutamate semialdehyde aminomutase,” Journal of Biological Chemistry, vol. 275, no. 6, pp. 3879–3886, 2000.
- J. L. Sorensen and J. Stetefeld, “Kinemage of action—proposed reaction mechanism of glutamate-1-semialdehyde aminomutase at an atomic level,” Biochemical and Biophysical Research Communications, vol. 413, no. 4, pp. 572–576, 2011.
- M. R. Eftink and C. A. Ghiron, “Fluorescence quenching studies with proteins,” Analytical Biochemistry, vol. 114, no. 2, pp. 199–227, 1981.
- E. Gratton and M. Limkeman, “A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution,” Biophysical Journal, vol. 44, no. 3, pp. 315–324, 1983.
- R. D. Spencer and G. Weber, “Measurements of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer,” Annals of the New York Academy of Sciences, vol. 158, pp. 361–376, 1969.
- D. M. Jameson and T. L. Hazlett, “Time resolved fluorescence in biology and biochemistry,” in Biophysical and Biochemical Aspects of Fluorescence Spectroscopy, T. G. Dewey, Ed., pp. 106–133, Plenum, New York, NY, USA, 1991.
- J. M. Beechem and E. Gratton, “Time-resolved laser spectroscopy in biochemistry,” in Proceedings of the SPIE, International Society for Optical Engineering, Bellingham, Wash, USA, 1988.
- M. R. Eftink, “The use of fluorescence methods to monitor unfolding transitions in proteins,” Biophysical Journal, vol. 66, no. 2 I, pp. 482–501, 1994.
- E. J. Faeder and G. G. Hammes, “Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme,” Biochemistry, vol. 10, no. 6, pp. 1041–1045, 1971.
- S. Benci, S. Vaccari, A. Mozzarelli, and P. F. Cook, “Time-resolved fluorescence of O-acetylserine sulfhydrylase,” Biochimica et Biophysica Acta, vol. 1429, no. 2, pp. 317–330, 1999.
- E. Salsi, R. Guan, B. Campanini et al., “Exploring O-acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy,” Archives of Biochemistry and Biophysics, vol. 505, no. 2, pp. 178–185, 2011.
- A. Mozzarelli and S. Bettati, “Exploring the pyridoxal 5′-phosphate-dependent enzymes,” Chemical Record, vol. 6, no. 5, pp. 275–287, 2006.
- A. Chattopadhyay, M. Meier, S. Ivaninskii et al., “Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes,” Biochemistry, vol. 46, no. 28, pp. 8315–8330, 2007.
- E. Salsi, B. Campanini, S. Bettati et al., “A two-step process controls the formation of the bienzyme cysteine synthase complex,” Journal of Biological Chemistry, vol. 285, no. 17, pp. 12813–12822, 2010.
- E. Pennacchietti, T. M. Lammens, G. Capitani et al., “Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH,” Journal of Biological Chemistry, vol. 284, no. 46, pp. 31587–31596, 2009.
- P. J. R. Lakowicz, Principles of Fluorescence Spectroscopy, Plenum Press, New York, NY, USA, 1983.
- S. Vaccari, S. Benci, A. Peracchi, and A. Mozzarelli, “Time-resolved fluorescence of tryptophan synthase,” Biophysical Chemistry, vol. 61, no. 1, pp. 9–22, 1996.
- M. Arrio-Dupont, “Fluorescence study of Schiff bases of pyridoxal. Comparison with L-aspartate aminotransferase,” Photochemistry and Photobiology, vol. 12, no. 4, pp. 297–315, 1970.
- E. Passera, B. Campanini, F. Rossi et al., “Human kynurenine aminotransferase II—reactivity with substrates and inhibitors,” FEBS Journal, vol. 278, no. 11, pp. 1882–1900, 2011.
- M. T. Olmo, F. Sánchez-Jiménez, M. A. Medina, and H. Hayashi, “Spectroscopic analysis of recombinant rat histidine decarboxylase,” Journal of Biochemistry, vol. 132, no. 3, pp. 433–439, 2002.
- S. Benci, S. Vaccari, A. Mozzarelli, and P. F. Cook, “Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates,” Biochemistry, vol. 36, no. 49, pp. 15419–15427, 1997.
- M. Bertoldi, B. Cellini, T. Clausen, and C. B. Voltattorni, “Spectroscopic and kinetic analyses reveal the pyridoxal 5′-phosphate binding mode and the catalytic features of Treponema denticola cystalysin,” Biochemistry, vol. 41, no. 29, pp. 9153–9164, 2002.
- B. Campanini, S. Raboni, S. Vaccari et al., “Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability,” Journal of Biological Chemistry, vol. 278, no. 39, pp. 37511–37519, 2003.
- A. N. Lane, “The accessibility of the active site and conformation states of the beta 2 subunit of tryptophan synthase studied by fluorescence quenching,” European Journal of Biochemistry, vol. 133, no. 3, pp. 531–538, 1983.
- M. R. Eftink and C. A. Ghiron, “Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies,” Biochemistry, vol. 15, no. 3, pp. 672–680, 1976.
- M. R. Eftink and C. A. Ghiron, “Fluorescence quenching of indole and model micelle systems,” Journal of Physical Chemistry, vol. 80, no. 5, pp. 486–493, 1976.
- S. Raboni, S. Bettati, and A. Mozzarelli, “Tryptophan synthase: a mine for enzymologists,” Cellular and Molecular Life Sciences, vol. 66, no. 14, pp. 2391–2403, 2009.
- S. P. Nair, J. L. Harwood, and R. A. John, “Direct identification and quantification of the cofactor in glutamate semialdehyde aminotransferase from pea leaves,” FEBS Letters, vol. 283, no. 1, pp. 4–6, 1991.
- S. Brody, J. S. Andersen, C. G. Kannangara, M. Meldgaard, P. Roepstorff, and D. Von Wettstein, “Characterization of the different spectral forms of glutamate 1-semialdehyde aminotransferase by mass spectrometry,” Biochemistry, vol. 34, no. 49, pp. 15918–15924, 1995.
- G. Fenalti, R. H. P. Law, A. M. Buckle et al., “GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop,” Nature Structural and Molecular Biology, vol. 14, no. 4, pp. 280–286, 2007.
- M. Bertoldi, M. Gonsalvi, R. Contestabile, and C. B. Voltattorni, “Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase,” Journal of Biological Chemistry, vol. 277, no. 39, pp. 36357–36362, 2002.
- P. Burkhard, C.-H. Tai, C. M. Ristroph, P. F. Cook, and J. N. Jansonius, “Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium,” Journal of Molecular Biology, vol. 291, no. 4, pp. 941–953, 1999.
- H. Tian, R. Guan, E. Salsi et al., “Identification of the structural determinants for the stability of substrate and aminoacrylate external schiff bases in O-acetylserine sulfhydrylase-A,” Biochemistry, vol. 49, no. 29, pp. 6093–6103, 2010.
- A. Mozzarelli, S. Bettati, B. Campanini et al., “The multifaceted pyridoxal 5′-phosphate-dependent O-acetylserine sulfhydrylase,” Biochimica et Biophysica Acta, vol. 1814, no. 11, pp. 1497–1510, 2011.
- S. Raboni, R. Contestabile, F. Spyrakis et al., “Pyridoxal 5′-phosphate-dependent enzymes: catalysis, conformation and genomics,” in Comprehensive Natural Products II Chemistry and Biochemistry, El Sevier, Oxford, UK, 2010.