Reaction mechanism and structural model of ADP-forming acetyl-CoA synthetase from the hyperthermophilic archaeon Pyrococcus furiosus: Evidence for a second active site histidine residue

Journal of Biological Chemistry

Volumn 283, Issue 22, 2008, Pages 15409-15418

  Bräsen, Christopher ^a   Schmidt, Marcel ^a   Grötzinger, Joachim ^a   Schönheit, Peter ^a  

^a UNIVERSITY OF KIEL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL REACTIONS; ENZYMES; MODEL STRUCTURES; PHOSPHORYLATION;

ACETYL PHOSPHATES; ACTIVE SITES; ARCHAEA; ATP SYNTHESIS; CATALYTIC SITES; DIPHOSPHATE; DOMAIN ORGANIZATIONS; ENZYME PHOSPHORYLATIONS; HISTIDINE RESIDUES; HYPERTHERMOPHILIC ARCHAEON; MOLECULAR PROPERTIES; MUTANT ENZYMES; PHOSPHORYL GROUPS; PYROCOCCUS FURIOSUS; REACTION MECHANISMS; SPATIAL ARRANGEMENTS; STRUCTURAL MODELS; SYNTHETASE; SYNTHETASES; WILD TYPES;

FORMING;

ACETYL COENZYME A; ACETYL COENZYME A SYNTHETASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; HISTIDINE; SUCCINYL COENZYME A SYNTHETASE; ACETATE COA LIGASE (ADP FORMING); ACETATE-COA LIGASE (ADP-FORMING); ACETYL PHOSPHATE; ARCHAEAL PROTEIN; LONG CHAIN FATTY ACID COENZYME A LIGASE; ORGANOPHOSPHATE;

ARTICLE; BETA CHAIN; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ENZYME SUBUNIT; KINETICS; PRIORITY JOURNAL; PYROCOCCUS FURIOSUS; REACTION ANALYSIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

ARCHAEA; PYROCOCCUS FURIOSUS;

ARCHAEAL PROTEINS; BINDING SITES; CATALYSIS; COENZYME A LIGASES; HISTIDINE; MODELS, MOLECULAR; PHOSPHORIC ACID ESTERS; PHOSPHORYLATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PYROCOCCUS FURIOSUS;

EID: 47249140922     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M710218200     Document Type: Article

References (38)

1. Reeves, R. E., Warren, L. G., Susskind, B., and Lo, H. S. (1977) J. Biol. Chem. 252, 726-731
2. Sanchez, L. B., and Müller, M. (1996) FEBS Lett. 378, 240-244
3. Schäfer, T., Selig, M., and Schönheit, P. (1993) Arch. Microbiol. 159, 72-83
4. Schönheit, P., and Schäfer, T. (1995) World J. Microbiol. Biotechnol. 11, 26-57
5. Bock, A. K., Glasemacher, J., Schmidt, R., and Schönheit, P. (1999) J. Bacteriol. 181, 1861-1867
6. Schäfer, T., and Schönheit, P. (1991) Arch. Microbiol. 155, 366-377
7. Siebers, B., and Schönheit, P. (2005) Curr. Opin. Microbiol. 8, 695-705
8. Mai, X., and Adams, M. W. W. (1996) J. Bacteriol. 178, 5897-5903
9. Sanchez, L. B., Morrison, H. G., Sogin, M. L., and Müller, M. (1999) Gene (Amst.) 233, 225-231
10. Musfeldt, M., Selig, M., and Schönheit, P. (1999) J. Bacteriol. 181, 5885-5888
11. Musfeldt, M., and Schönheit, P. (2002) J. Bacteriol. 184, 636-644
12. Bräsen, C., and Schönheit, P. (2004) Arch. Microbiol. 182, 277-287
13. Sanchez, L. B., Galperin, M. Y., and Müller, M. (2000) J. Biol. Chem. 275, 5794-5803
14. Elshourbagy, N. A., Near, J. C., Kmetz, P. J., Wells, T. N., Groot, P. H., Saxty, B. A., Hughes, S. A., Franklin, M., and Gloger, I. S. (1992) Eur. J. Biochem. 204, 491-499
15. Chistoserdova, L. V., and Lidstrom, M. E. (1994) J. Bacteriol. 176, 7398-7404
16. Binieda, A., Fuhrmann, M., Lehner, B., Rey-Berthod, C., Frutiger-Hughes, S., Hughes, G., and Shaw, N. M. (1999) Biochem. J. 340, 793-801
17. Plaggenborg, R., Steinbüchel, A., and Priefert, H. (2001) FEMS Microbiol. Lett. 205, 9-16
18. Fraser, M. E., James, M. N., Bridger, W. A., and Wolodko, W. T. (1999) J. Mol. Biol. 285, 1633-1653
19. Fraser, M. E., Joyce, M. A., Ryan, D. G., and Wolodko, W. T. (2002) Biochemistry 41, 537-546
20. Wolodko, W. T., Fraser, M. E., James, M. N., and Bridger, W. A. (1994) J. Biol. Chem. 269, 10883-10890
21. Marchler-Bauer, A., and Bryant, S. H. (2004) Nucleic Acids Res. 32, 327-331
22. Majumdar, R., Guest, J. R., and Bridger, W. A. (1991) Biochim. Biophys. Acta 1076, 86-90
23. Marchler-Bauer, A., Anderson, J. B., Cherukuri, P. F., Weese-Scott, C., Geer, L. Y., Gwadz, M., He, S., Hurwitz, D. I., Jackson, J. D., Ke, Z., Lanczycki, C. J., Liebert, C. A., Liu, C., Lu, F., Marchler, G. H., Mullokandov, M., Shoemaker, B. A., Simonyan, V., Song, J. S., Thiessen, P. A., Yamashita, R. A., Yin, J. J., Zhang, D., and Bryant, S. H. (2005) Nucleic Acids Res. 33, 192-196
24. Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) Nucleic Acids Res. 25, 4876-4882
25. Vriend, G. (1990) J. Mol. Graph. 8, 29 and 52-56
26. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
27. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467
28. Srere, P. A., Brazil, H., and Gonen, L. (1963) Acta Chem. Scand. 17, 129-134
29. Chen, G. C., and Yang, J. T. (1977) Anal. Lett. 10, 1195-1207
30. Lehtiö, L., Fabrichniy, I., Hansen, T., Schönheit, P., and Goldman, A. (2005) Acta Crystallogr. D Biol. Crystallogr. 61, 350-354
31. Shikata, K., Fukui, T., Atomi, H., and Imanaka, T. (2007) J. Biol. Chem. 282, 26963-26970
32. Weitzman, P. D., and Kinghorn, H. A. (1978) FEBS Lett. 88, 255-258
33. Bailey, D. L., Fraser, M. E., Bridger, W. A., James, M. N., and Wolodko, W. T. (1999) J. Mol. Biol. 285, 1655-1666
34. Fraser, M. E., James, M. N., Bridger, W. A., and Wolodko, W. T. (2000) J. Mol. Biol. 299, 1325-1339
35. Kanao, T., Fukui, T., Atomi, H., and Imanaka, T. (2002) Eur. J. Biochem. 269, 3409-3416
36. Joyce, M. A., Fraser, M. E., James, M. N., Bridger, W. A., and Wolodko, W. T. (2000) Biochemistry 39, 17-25
37. Fraser, M. E., Hayakawa, K., Hume, M. S., Ryan, D. G., and Brownie, E. R. (2006) J. Biol. Chem. 281, 11058-11065
38. Pearson, P. H., and Bridger, W. A. (1975) J. Biol. Chem. 250, 8524-8529