Asymmetry of the active site loop conformation between subunits of glutamate-1-semialdehyde aminomutase in solution

BioMed Research International

Volumn 2013, Issue , 2013, Pages

  Campanini, Barbara ^a   Bettati, Stefano ^a,b   Di Salvo, Martino Luigi ^c   Mozzarelli, Andrea ^a,b   Contestabile, Roberto ^c  

^a UNIVERSITY OF PARMA   (Italy)

^b NATIONAL INSTITUTE OF BIOSTRUCTURES AND BIOSYSTEMS   (Italy)

^c SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE 1 SEMIALDEHYDE AMINOMUTASE; POTASSIUM IODIDE; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG; COENZYME; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; MUTASE; PROTEIN SUBUNIT; PYRIDOXAMINE; SOLUTION AND SOLUBILITY; GLUTAMATE 1 SEMIALDEHYDE 2,1 AMINOMUTASE;

ARTICLE; CATALYSIS; CONFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ELECTROSPRAY MASS SPECTROMETRY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PROTEIN EXPRESSION; ABSORPTION; BIOCATALYSIS; CHEMISTRY; COENZYME; DRUG EFFECTS; ENZYMOLOGY; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SUBUNIT; SOLUTION AND SOLUBILITY; SPECTROFLUOROMETRY; SYNECHOCOCCUS; X RAY CRYSTALLOGRAPHY; DRUG EFFECT;

ABSORPTION; BIOCATALYSIS; CATALYTIC DOMAIN; COENZYMES; CRYSTALLOGRAPHY, X-RAY; INTRAMOLECULAR TRANSFERASES; POTASSIUM IODIDE; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; PYRIDOXAL PHOSPHATE; PYRIDOXAMINE; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; SYNECHOCOCCUS;

EID: 84883199592     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/353270     Document Type: Article

References (50)

1. Jordan P. M., Shemin D., δ -Aminolevulinic Acid Synthetase, in the Enzymes 1972 New York, NY, USA Academic Press
2. Beale S. I., Weinstein J. D., Biosynthesis of Haem and Chlorophylls 1990 New York, NY, USA McGraw-Hill
3. Kannangara C. G., Gough S. P., Bruyant P., Hoober J. K., Kahn A., von Wettstein D., tRNA(Glu) as a cofactor in delta-aminolevulinate biosynthesis: steps that regulate chlorophyll synthesis. Trends in Biochemical Sciences 1988 13 139 143
4. Grishin N. V., Phillips M. A., Goldsmith E. J., Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Science 1995 4 1291 1304
5. Contestabile R., Jenn T., Akhtar M., Gani D., John R. A., Reactions of glutamate 1-semialdehyde aminomutase with R- and S- enantiomers of a novel, mechanism-based inhibitor, 2,3-diaminopropyl sulfate. Biochemistry 2000 39 11 3091 3096 2-s2.0-0034696678 10.1021/bi992307k
6. Smith M. A., Kannangara C. G., Grimm B., Von Wettstein D., Characterization of glutamate-1-semialdehyde aminotransferase of Synechococcus. Steady-state kinetic analysis. European Journal of Biochemistry 1991 202 3 749 757 2-s2.0-0026354418
7. Smith M. A., Grimm B., Kannangara C. G., Von Wettstein D., Spectral kinetics of glutamate-1-semialdehyde aminomutase of Synechococcus. Proceedings of the National Academy of Sciences of the United States of America 1991 88 21 9775 9779 2-s2.0-0026004643
8. Pugh C. E., Harwood J. L., John R. A., Mechanism of glutamate semialdehyde aminotransferase: roles of diamino- and dioxo-intermediates in the synthesis of aminolevulinate. Journal of Biological Chemistry 1992 267 3 1584 1588 2-s2.0-0026567122
9. Christen P., Metzler D. E., Transaminases 1995 New York, NY, USA Wiley
10. Tyacke R. J., Harwood J. L., John R. A., 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 1993 293 part 3 697 701 2-s2.0-0027200684
11. Grimm B., Smith A. J., Kannangara C. G., Smith M., 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 1991 266 19 12495 12501 2-s2.0-0025776781
12. Ilag L. L., Jahn D., Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R. Biochemistry 1992 31 31 7143 7151 2-s2.0-0026784537
13. D'Aguanno S., Gonzales I. N., Simmaco M., Contestabile R., John R. A., Stereochemistry of the reactions of glutamate-1-semialdehyde aminomutase with 4,5-diaminovalerate. Journal of Biological Chemistry 2003 278 42 40521 40526 2-s2.0-0142103654 10.1074/jbc.M306223200
14. Hennig M., Grimm B., Contestabile R., John R. A., Jansonius J. N., Crystal structure of glutamate-1-semialdehyde aminomutase: an α 2-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 1997 94 10 4866 4871 2-s2.0-0030995422
15. Stetefeld J., Jenny M., Burkhard P., Intersubunit signaling in glutamate-1-semialdehyde-aminomutase. Proceedings of the National Academy of Sciences of the United States of America 2006 103 37 13688 13693 2-s2.0-33748796388 10.1073/pnas.0600306103
16. Contestabile R., Angelaccio S., Maytum R., Bossa F., John R. A., The contribution of a conformationally mobile, active site loop to the reaction catalyzed by glutamate semialdehyde aminomutase. Journal of Biological Chemistry 2000 275 6 3879 3886 2-s2.0-0034635371 10.1074/jbc.275.6.3879
17. Sorensen J. L., Stetefeld J., Kinemage of action-proposed reaction mechanism of glutamate-1-semialdehyde aminomutase at an atomic level. Biochemical and Biophysical Research Communications 2011 413 4 572 576 2-s2.0-80053611863 10.1016/j.bbrc.2011.09.003
18. Eftink M. R., Ghiron C. A., Fluorescence quenching studies with proteins. Analytical Biochemistry 1981 114 2 199 227 2-s2.0-0019593952
19. Gratton E., Limkeman M., A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution. Biophysical Journal 1983 44 3 315 324 2-s2.0-0020997959
20. Spencer R. D., Weber G., Measurements of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer. Annals of the New York Academy of Sciences 1969 158 361 376
21. Jameson D. M., Hazlett T. L., Dewey T. G., Time resolved fluorescence in biology and biochemistry. Biophysical and Biochemical Aspects of Fluorescence Spectroscopy 1991 New York, NY, USA Plenum 106 133
22. Beechem J. M., Gratton E., Time-resolved laser spectroscopy in biochemistry. Proceedings of the SPIE 1988 Bellingham, Wash, USA International Society for Optical Engineering
23. Eftink M. R., The use of fluorescence methods to monitor unfolding transitions in proteins. Biophysical Journal 1994 66 2 I 482 501 2-s2.0-0027958069
24. Faeder E. J., Hammes G. G., Kinetic studies of tryptophan synthetase. Interaction of L-serine, indole, and tryptophan with the native enzyme. Biochemistry 1971 10 6 1041 1045 2-s2.0-0015228604
25. Benci S., Vaccari S., Mozzarelli A., Cook P. F., Time-resolved fluorescence of O -acetylserine sulfhydrylase. Biochimica et Biophysica Acta 1999 1429 2 317 330 2-s2.0-0032899686 10.1016/S0167-4838(98)00229-5
26. Salsi E., Guan R., Campanini B., Bettati S., Lin J., Cook P. F., Mozzarelli A., Exploring O -acetylserine sulfhydrylase-B isoenzyme from Salmonella typhimurium by fluorescence spectroscopy. Archives of Biochemistry and Biophysics 2011 505 2 178 185 2-s2.0-78651229570 10.1016/j.abb.2010.10.005
27. Mozzarelli A., Bettati S., Exploring the pyridoxal 5′-phosphate- dependent enzymes. Chemical Record 2006 6 5 275 287 2-s2.0-33846236550 10.1002/tcr.20094
28. Chattopadhyay A., Meier M., Ivaninskii S., Burkhard P., Speroni F., Campanini B., Bettati S., Mozzarelli A., Rabeh W. M., Li L., Cook P. F., Structure, mechanism, and conformational dynamics of O -acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry 2007 46 28 8315 8330 2-s2.0-34447554594 10.1021/bi602603c
29. Salsi E., Campanini B., Bettati S., Raboni S., Roderick S. L., Cook P. F., Mozzarelli A., A two-step process controls the formation of the bienzyme cysteine synthase complex. Journal of Biological Chemistry 2010 285 17 12813 12822 2-s2.0-77951212184 10.1074/jbc.M109.075762
30. Pennacchietti E., Lammens T. M., Capitani G., Franssen M. C. R., John R. A., Bossa F., De Biase D., 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 2009 284 46 31587 31596 2-s2.0-70450233413 10.1074/jbc.M109.049577
31. Lakowicz P. J. R., Principles of Fluorescence Spectroscopy 1983 New York, NY, USA Plenum Press
32. Vaccari S., Benci S., Peracchi A., Mozzarelli A., Time-resolved fluorescence of tryptophan synthase. Biophysical Chemistry 1996 61 1 9 22 2-s2.0-0030606789 10.1016/0301-4622(96)00020-8
33. Arrio-Dupont M., Fluorescence study of Schiff bases of pyridoxal. Comparison with L-aspartate aminotransferase. Photochemistry and Photobiology 1970 12 4 297 315 2-s2.0-0014860265
34. Passera E., Campanini B., Rossi F., Casazza V., Rizzi M., Pellicciari R., Mozzarelli A., Human kynurenine aminotransferase II-reactivity with substrates and inhibitors. FEBS Journal 2011 278 11 1882 1900 2-s2.0-79956205060 10.1111/j.1742-4658.2011.08106.x
35. Olmo M. T., Sánchez-Jiménez F., Medina M. A., Hayashi H., Spectroscopic analysis of recombinant rat histidine decarboxylase. Journal of Biochemistry 2002 132 3 433 439 2-s2.0-0036737948
36. Benci S., Vaccari S., Mozzarelli A., Cook P. F., Time-resolved fluorescence of O -acetylserine sulfhydrylase catalytic intermediates. Biochemistry 1997 36 49 15419 15427 2-s2.0-0030722376 10.1021/bi970464i
37. Bertoldi M., Cellini B., Clausen T., Voltattorni C. B., Spectroscopic and kinetic analyses reveal the pyridoxal 5′-phosphate binding mode and the catalytic features of Treponema denticola cystalysin. Biochemistry 2002 41 29 9153 9164 2-s2.0-0037162435 10.1021/bi025649q
38. Campanini B., Raboni S., Vaccari S., Zhang L., Cook P. F., Hazlett T. L., Mozzarelli A., Bettati S., Surface-exposed tryptophan residues are essential for O -acetylserine sulfhydrylase structure, function, and stability. Journal of Biological Chemistry 2003 278 39 37511 37519 2-s2.0-0141621191 10.1074/jbc.M305138200
39. Lane A. N., 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 1983 133 3 531 538 2-s2.0-0020788861
40. Eftink M. R., Ghiron C. A., Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 1976 15 3 672 680 2-s2.0-0017288499
41. Eftink M. R., Ghiron C. A., Fluorescence quenching of indole and model micelle systems. Journal of Physical Chemistry 1976 80 5 486 493 2-s2.0-33847798446
42. Raboni S., Bettati S., Mozzarelli A., Tryptophan synthase: a mine for enzymologists. Cellular and Molecular Life Sciences 2009 66 14 2391 2403 2-s2.0-67650409780 10.1007/s00018-009-0028-0
43. Nair S. P., Harwood J. L., John R. A., Direct identification and quantification of the cofactor in glutamate semialdehyde aminotransferase from pea leaves. FEBS Letters 1991 283 1 4 6 2-s2.0-0025759034 10.1016/0014-5793(91) 80540-J
44. Brody S., Andersen J. S., Kannangara C. G., Meldgaard M., Roepstorff P., Von Wettstein D., Characterization of the different spectral forms of glutamate 1-semialdehyde aminotransferase by mass spectrometry. Biochemistry 1995 34 49 15918 15924 2-s2.0-0028826262 10.1021/bi00049a006
45. Fenalti G., Law R. H. P., Buckle A. M., Langendorf C., Tuck K., Rosado C. J., Faux N. G., Mahmood K., Hampe C. S., Banga J. P., Wilce M., Schmidberger J., Rossjohn J., El-Kabbani O., Pike R. N., Smith A. I., Mackay I. R., Rowley M. J., Whisstock J. C., GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nature Structural and Molecular Biology 2007 14 4 280 286 2-s2.0-34247249781 10.1038/nsmb1228
46. Bertoldi M., Gonsalvi M., Contestabile R., Voltattorni C. B., Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase. Journal of Biological Chemistry 2002 277 39 36357 36362 2-s2.0-0037184097 10.1074/jbc.M204867200
47. Burkhard P., Tai C.-H., Ristroph C. M., Cook P. F., Jansonius J. N., Ligand binding induces a large conformational change in O -acetylserine sulfhydrylase from Salmonella typhimurium. Journal of Molecular Biology 1999 291 4 941 953 2-s2.0-0033609810 10.1006/jmbi.1999.3002
48. Tian H., Guan R., Salsi E., Campanini B., Bettati S., Kumar V. P., Karsten W. E., Mozzarelli A., Cook P. F., Identification of the structural determinants for the stability of substrate and aminoacrylate external schiff bases in O -acetylserine sulfhydrylase-A. Biochemistry 2010 49 29 6093 6103 2-s2.0-77954823582 10.1021/bi100473v
49. Mozzarelli A., Bettati S., Campanini B., Salsi E., Raboni S., Singh R., Spyrakis F., Kumar V. P., Cook P. F., The multifaceted pyridoxal 5′-phosphate-dependent O -acetylserine sulfhydrylase. Biochimica et Biophysica Acta 2011 1814 11 1497 1510 2-s2.0-80054687027 10.1016/j.bbapap.2011. 04.011
50. Raboni S., Contestabile R., Spyrakis F., Campanini B., Amadasi A., Bettati S., Peracchi A., Mozzarelli A., Pyridoxal 5′-phosphate-dependent enzymes: catalysis, conformation and genomics. Comprehensive Natural Products II Chemistry and Biochemistry 2010 Oxford, UK El Sevier