31P NMR spectroscopy senses the microenvironment of the 5′-phosphate group of enzyme-bound pyridoxal 5′-phosphate

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1814, Issue 11, 2011, Pages 1447-1458

  Schnackerz, Klaus D ^a   Andi, Babak ^b   Cook, Paul F ^b  

^a UNIVERSITY OF WÜRZBURG   (Germany)

^b UNIVERSITY OF OKLAHOMA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE AMINOTRANSFERASE; CARBOXYLYASE; CYSTEINE SYNTHASE; LYSINE; PYRIDOXAL 5 PHOSPHATE; SCHIFF BASE; SERINE DEHYDRATASE; SOLVENT; TRYPTOPHAN SYNTHASE; TRYPTOPHANASE;

ENZYME BINDING; ENZYME KINETICS; MICROENVIRONMENT; MUTATION; NONHUMAN; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT; REVIEW;

CATALYSIS; ENZYMES; GLYCINE; MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHORUS ISOTOPES; PYRIDOXAL PHOSPHATE;

EID: 80054701935     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.02.001     Document Type: Review

References (43)

1. D.G. Gorenstein Dependence of phosphorus-31 chemical shift on oxygen-phosphorus-oxygen bond angles in phosphate esters J. Am. Chem. Soc. 97 1975 898 900
2. K.D. Schnackerz, and K. Feldmann Pyridoxal 5′- deoxymethylenephosphonate reconstituted D-serine dehydratase: a phosphorus-31 nuclear magnetic resonance study Biochem. Biophys. Res. Commun. 95 1983 1832 1838
3. 6 and Derivatives, Pyridoxal Phosphate Vol. 1 1986 Wiley Interscience New York 245 264 part A
4. K.D. Schnackerz, and G. Waldmann T. Fukui, H. Kagamiyama, K. Soda, H. Wada, Enzymes dependent on pyridoxal phosphate and other carbonyl compounds 1991 Pergamon Press New York 149 152
5. H.J. Vogel, W.A. Bridger, and B.D. Sykes Frequency-dependent phosphorus-31 nuclear magnetic resonance studies of the phosphohistidine residue of succinyl-CoA synthase and the phosphoserine residue of glycogen phosphorylase Biochemistry 21 1982 1126 1132
6. 31P NMR is a sensitive indicator of small conformational changes in the coenzyme of aspartate aminotrasferase Eur. J. Biochem. 185 1989 525 531 (Pubitemid 20009153)
7. K.D. Schnackerz Phosphorus-31 nuclear magnetic resonance study on cytoplasmic aspartate aminotransferase from pig heart Biochem. Biophys. Acta 789 1984 241 244
8. D.M. Kiick, and P.F. Cook pH studies towards elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase Biochemistry 22 1983 375 382
9. C.A. Lamartiniere, H. Itoh, and W.B. Dempsey ω-Dialkylamino acid transaminase from Pseudomonas cepacia. Purification, crystallization, physical, and kinetic properties Biochemistry 10 1971 4783 4788
10. H.G. Aalesstad, J.P. Bouis Jr., A.T. Philips, and A.D. Larson Characterization of a decarboxylation dependent transaminase E.E. Snell, A.E. Braunstein, E.S. Severin, Y.M. Torchinsky, Pyridoxal catalysis: enzymes and model systems 1968 Wiley Interscience New York 479 490
11. W.K. Maas, and B.D. Davis Pantothenate studies: I. Interference by D-serine and L-aspartate with pantothenate synthase in Escherichia coli J. Bacteriol. 60 1950 733 740
12. W. Dowhan Jr., and E.E. Snell D-Serine dehydratase from Escherichia coli: II. Analytical studies and subunit structure J. Biol. Chem. 245 1970 4618 4628
13. M. Marceau, E. McFall, S.D. Lewis, and J.A. Shafer D-Serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants J. Biol. Chem. 263 1988 16926 16933 (Pubitemid 18268876)
14. K.D. Schnackerz, K. Feldmann, and W.E. Hull Phosphorus-31 nuclear magnetic resonance study of D-serine dehydratase: pyridoxal phosphate binding site Biochemistry 18 1979 1536 1539
15. W.E. Hull, and B.D. Sykes Fluorotyrosine alkaline phosphatase: Internal mobility of individual tyrosines and the role of chemical shift anisotropy as a 19F nuclear spin relaxation mechanism in Proteins J. Mol. Biol. 98 1975 121 152
16. 31P NMR spectroscopy Biochem. Biophys. Acta 1764 2006 230 238
17. E. Hohenester, J.W. Keller, and J.N. Jansonius An alkali metal ion size dependent switch in the active site of dialkylglcine decarboxylase Biochemistry 33 1994 13561 13570 (Pubitemid 24381918)
18. M.D. Toney, E. Hohenester, J.W. Keller, and J.N. Jansonius Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase J. Mol. Biol. 245 1995 151 179
19. T. Yamada, J. Komoto, Y. Takata, H. Ogawa, H.C. Pitot, and F. Takusagawa Crystal structure of serine dehydratase from rat liver Biochemistry 42 2003 12854 12865 (Pubitemid 37385816)
20. Y. Morino, and E.E. Snell The relation of spectral changes and tritium exchange reactions to the mechanism of tryptophanase-catalyzed reactions J. Biol. Chem. 242 1967 2800 2809
21. K.D. Schnackerz, and E.E. Snell Phosphorus-31 nuclear magnetic resonance study of tryptophanase, pyridoxal phosphate-binding site J. Biol. Chem. 258 1983 4839 4841
22. N.M. Kredich, and G.M. Tomkins The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium J. Biol. Chem. 241 1966 4955 4965
23. M. Filutowicz, A. Waiter, and D. Hulanicka Delayed inducibility of sulfite reductase in CysM mutants of Salmonella typhimurium under anaerobic conditions J. Gen. Microbiol. 128 1982 1791 1794 (Pubitemid 12001916)
24. 31P NMR spectra of O-acetylserine sulfhydrylase in the absence of and presence of O-acetylserine Biochemistry 31 1992 2298 2303
25. 31P NMR spectroscopy Protein Pept. Lett. 7 2000 207 210
26. E. Woehl, C.-H. Tai, M.F. Dunn, and P.F. Cook Rapid scanning stopped-flow studies of O-acetylserine sulfhydrylase indicate a rate-determining first half reaction Biochemistry 35 1996 4776 4783
27. K.D. Schnackerz, C.-H. Tai, J.W. Simmons III, M. Jacobson, G.S.J. Rao, and P.F. Cook Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction Biochemistry 34 1995 12152 12160
28. C.-H. Tai, W.M. Rabeh, R. Guan, K.D. Schnackerz, and P.F. Cook Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction Arch. Biochem. Biophys. 472 2008 115 125
29. P. Burkhard, G.S.J. Rao, E. Hohenester, K.D. Schnackerz, P.F. Cook, and J.N. Jansonius The three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium at 2.2 Å J. Mol. Biol. 283 1998 121 123
30. C.-H. Tai, W.M. Rabeh, R. Guan, K.D. Schnackerz, and P.F. Cook Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium Biochem. Biophys. Acta 1784 2008 629 637
31. 31P NMR Studies of O-acetylserine sulfhydrylase-B from Salmonella typhimurium Arch. Biochem. Biophys. 487 2009 85 90
32. A. Chattopadhyay, M. Meier, S. Ivaninskii, P. Burkhard, F. Speroni, B. Campanini, S. Bettati, A. Mozarelli, W.M. Rabeh, L. Li, and P.F. Cook Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes Biochemistry 46 2007 8315 8330 (Pubitemid 47075970)
33. 6, Pyridoxal Phosphate Vol. 1 1986 253 310 part B
34. 31P NMR spectroscopy J. Biol. Chem. 273 1998 33247 33253
35. S. Raboni, A. Mozzarelli, and P.F. Cook Control of ionizable residues in the catalytic mechanism of tryptophan synthase from Salmonella typhimurium Biochemistry 46 2007 13235 13244
36. K.D. Schnackerz, and P. Bartholmes Phosphorus-31 nuclear magnetic resonance study of pyridoxal 5′-phosphate binding to Escherichia coli tryptophan synthase Biochem. Biophys. Res. Commun. 111 1983 817 823 (Pubitemid 13081828)
37. P. Bartholmes, G. Lentzen, B. Reckmann, T. Schwarz, and K.D. Schnackerz Indol propanol phosphate as a conformational probe in various forms of E. coli tryptophan synthase: a phosphorus-31 NMR study T. Fukui, H. Kagamiyama, K. Soda, H. Wada, Enzymes dependent on pyridoxal phosphate and other carbonyl compounds 1991 Pergamon Press New York 269 271
38. H. Enei, H. Matsui, K. Ymashita, S. Okumura, and H. Yamada Elimination, replacement and isomerization reactions by intact cells containing tyrosine phenol-lyase Agric. Biol. Chem. 36 1972 1861 1868
39. V.K. Kazakov, I.I. Tarusina, I.V. Myagkikh, and T.V. Demidkina Identity of tyrosine phenol-lyase from Citrobacter intermedius subunits Biokhimiya (Moscow) 52 1987 1319 1323
40. B. Sundararaju, H. Chen, S. Shilicutt, and R.S. Phillips The role of glutamic acid-69 in the activation of Citrobacter freundii tyrosine phenol-lyase by monovalent cations Biochemistry 39 2000 8548 8555
41. B. Sundararaju, A.A. Antson, R.S. Philipps, T.V. Demidkina, M.V. Barbolina, P. Gollnick, G.G. Dodson, and K.S. Wilson The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3- (4′hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity Biochemistry 36 1997 6502 6510 (Pubitemid 27231409)
42. M.N. Isupov, A.A. Antson, E.J. Dodson, G.G. Dodson, I.S. Dementieva, L.N. Zakomirdina, K.S. Wilson, Z. Dauter, A.A. Lebedew, and E.H. Harutyunyan Crystal structure of tryptophanase J. Mol. Biol. 276 1998 603 623 (Pubitemid 28116133)
43. V.N. Malashkevich, P. Strop, J.W. Keller, J.N. Jansonius, and M.D. Toney Crystal structures of dialkylglycine decarboxylase inhibitors J. Mol. Biol. 294 1999 193 200