The stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the α-protons of amino acids

Biochemical Journal

Volumn 381, Issue 3, 2004, Pages 847-852

  Níbeilliú, Máire E ^a   Malthouse, J Paul G ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

Author keywords

proton; Hydrogen deuterium exchange; NMR; Stereospecificity; Tryptophan synthase

Indexed keywords

CATALYSIS; DEUTERIUM; HYDROGEN; NUCLEAR MAGNETIC RESONANCE; PARAMETER ESTIMATION; PROTONS;

ELECTRONEGATIVITY; SERINES; STEREOSPECIFICITY; TRYPTOPHAN SYNTHASE;

AMINO ACIDS;

AMINO ACID; DEUTERIUM; DEXTRO AMINO ACID; NORLEUCINE; PROTON; SERINE; TRYPTOPHAN; TRYPTOPHAN SYNTHASE;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; ELECTRICITY; PH; PRIORITY JOURNAL; PROTON TRANSPORT; STEREOSPECIFICITY;

ALANINE; AMINO ACIDS; AMINOBUTYRIC ACIDS; CATALYSIS; DEUTERIUM; GLYCINE HYDROXYMETHYLTRANSFERASE; HYDROGEN; KINETICS; NORLEUCINE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PREDICTIVE VALUE OF TESTS; PROTONS; SERINE; STEREOISOMERISM; SUBSTRATE SPECIFICITY; TRYPTOPHAN; TRYPTOPHAN SYNTHASE; VALINE;

EID: 4344620030     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040388     Document Type: Article

References (29)

1. Malthouse, J. P. G. (1999) Using NMR as a probe of protein structure and function. Biochem. Soc. Trans. 27, 701-713
2. Malthouse, J. P. G. (2003) Stereospecificity of α-proton exchange reactions catalysed by pyridoxal-5′-phosphate dependent enzymes. Biochim. Biophys. Acta 1647, 138-142
3. Fitzpatrick, T. B. and Malthouse, J. P. G. (1996) Proof that serine hydroxymethyltransferase retains its specificity for the pro-2S proton of glycine in the absence of tetrahydrofolate. Biochem. Soc. Trans. 24, 132S
4. Fitzpatrick, T. B. and Malthouse, J. P. G. (1998) A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalysed exchange of the α-protons of amino acids - evidence for a second catalytic site. Eur. J. Biochem. 252, 113-117
5. Malthouse, J. P. G., Milne, J. J. and Gariani, L. S. (1991) A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine. Biochem. J. 274, 807-812
6. Mahon, M. M., Gramatikova, S. I., Christen, P., Fitzpatrick, T. B. and Malthouse, J. P. G. (1998) The pyridoxal-5′-phosphate-dependenf catalytic antibody 15A9: its efficiency and stereospecificity in catalysing the exchange of the α-protons of glycine. FEBS Lett. 427, 74-78
7. Mahon, M. M., Graber, R., Christen, P. and Malthouse, J. P. G. (1999) The aspartate aminotransferase-catalysed exchange of the α-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction. Biochim. Biophys. Acta 1434, 191-201
8. Milne, J. J. and Malthouse, J. P. G. (1993) A study of the tryptophan synthase catalysed H/D exchange of the α-protons of amino acids. Biochem. Soc. Trans. 22, 43S
9. Milne, J. J. and Malthouse, J. P. G. (1995) Factors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine. Biochem. J. 311, 1015-1019
10. Milne, J. J. and Malthouse, J. P. G. (1996) The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the α-protons of amino acids. Biochem. J. 314, 787-791
11. Milne, J. J. and Malthouse, J. P. G. (1996) Enzymatic synthesis of α-deuterated amino acids. Biochem. Soc. Trans. 24, 1335
12. Dunathan, H. C. (1966) Conformation and reaction specificity in pyridoxal phosphate enzymes. Proc. Natl. Acad. Sci. U.S.A. 55, 712-716
13. Houben, K. F. and Dunn, M. F. (1990) Allosteric effects acting over a distance of 20-25 Å in the Escherichia coli tryptophan synthase bienzyme complex increase ligand affinity and cause redistribution of covalent intermediates. Biochemistry 29, 2421-2429
14. Brzovic, P. S., Sawa, Y., Hyde, C. C., Miles, E. W. and Dunn, M. F. (1992) Evidence that mutations in a loop region of the α-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex. J. Biol. Chem. 267, 13028-13038
15. Dunn, M. F., Aguilar, V., Brzovic, P., Drewe, W. F. J., Houben, K. F., Leja, C. A. and Roy, M. (1990) The tryptophan synthase bienzyme complex transfers indole between the α- and β-sites via a 25-30 Å long tunnel. Biochemistry 29, 8598-8607
16. +-activated tryptophan synthase bienzyme complex. Biochemistry 41, 9982-9990
17. Miles, E. W., Kawasaki, H., Ahmed, S. A., Morita, H. and Nagata, N. (1989) The β subunit of tryptophan synthase, clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170 and cysteine 230. J. Biol. Chem. 264, 6280-6287
18. Yang, L. H., Ahmed, S. A. and Miles, E. W. (1996) PCR mutagenesis and over expression of tryptophan synthase from Salmonella typhimurium on the roles of β2 subunit Lys-382. Protein Expression Purif. 8, 126-136
19. Henning, U., Helinski, D. R., Chao, F. C. and Yanofsky, C. (1962) The A protein of the tryptophan synthetase of Escherichia coli. J. Biol. Chem. 237, 1523-1530
20. Miles, E. W., Bauerle, R. and Ahmed, S. A. (1987) Tryptophan synthase from Escherichia coli and Salmonella typhimurium. Methods Enzymol. 142, 398-414
21. Hogberg-Raibaud, A. and Goldberg, M. E. (1977) Isolation and characterization of independently folding regions of the β chain of Escherichia coli tryptophan synthetase. Biochemistry 16, 4014-4020
22. Vold, R. L., Waugh, J. S., Klein, M. P. and Phelps, D. E. (1968) Measurement of spin relaxation in complex systems. J. Chem. Phys. 48, 3831-3832
23. Malthouse, J. P. G., Milne, J. J., Fitzpatrick, T. B. and Mahon, M. M. (1996) Kinetic analysis of the exchange of the α-protons of amino acids by pyridoxal-phosphate-dependent enzymes. Biochem. Soc. Trans. 24, 134S
24. Malthouse, J. P. G., Fitzpatrick, T. B. and Mahon, M. M. (1998) A comparison of some of the methods available for analysing the substrate dependence of the exchange of the α-protons of amino acids catalysed by pyridoxal-phosphate-dependent enzymes. Biochem. Soc. Trans. 26, 66
25. Brzovic, P. S., Ngo, K. and Dunn, M. F. (1992) Allosteric interactions coordinate catalytic activity between successive metabolic enzymes in the tryptophan synthase bienzyme complex. Biochemistry 31, 3831-3839
26. Lane, A. N. and Kirschner, K. (1981) The mechanism of tryptophan binding to tryptophan synthase from Escherichia coli. Eur. J. Biochem. 120, 379-387
27. Lane, A. N. and Kirschner, K. (1983) The mechanism of binding of L-serine to tryptophan synthase from Escherichia coli. Eur. J. Biochem. 129, 561-570
28. Richard, J. P. and Amyes, T. L. (2001) Proton transfer at carbon. Curr. Opin. Chem. Biol. 5, 623-633
29. a Prediction for Organic Acids and Bases, Chapman and Hall, London and New York