On the Conformation of the Substrate Binding to the Active Site during the Course of Enzymatic Decarboxylation

Bulletin of the Chemical Society of Japan

Volumn 69, Issue 12, 1996, Pages 3591-3594

  Kawasaki, Takayasu ^a   Horimai, Emiko ^a   Ohta, Hiromichi ^a  

^a KEIO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0010553011     PISSN: 00092673     EISSN: None     Source Type: Journal    
DOI: 10.1246/bcsj.69.3591     Document Type: Article

References (29)

1. a) K. Miyamoto and H. Ohta, J. Am. Chem. Soc., 112, 4077 (1990);
2. b) K. Miyamoto and H. Ohta, Eur. J. Biochem., 210, 475 (1992).
3. a) T. Kawasaki, M. Watanabe, and H. Ohta, Bull. Chem. Soc. Jpn., 68, 2017 (1995);
4. b) T. Kawasaki, Y. Fujioka, K. Saito, and H. Ohta, Chem Lett., 1996, 195.
5. Carbanion intermediates in enzyme reactions have also been claimed in the case of mandelate recemase and muconate lactonizing enzyme.
6. a) G. D. Hegeman, E. Y. Rosenberg, and G. L. Kenyon, Biochemistry, 9, 4029 (1970);
7. b) D. J. Neidhart, G. L. Kenyon, J. A. Gerlt, and G. A. Petsko, Nature, 347, 692 (1990).
8. K. Miyamoto, H. Ohta, and Y. Osamura, Bioorg. Med. Chem., 2, 469 (1994).
9. C-C bond between the phenyl ring and α-carbon is now focused on discussion.
10. a) I. B. Wilson and E. Cabib, J. Am. Chem. Soc., 78, 202 (1956);
11. b) M. L. Bender, F. J. Kezdy, and C. R. Gunter, J. Am. Chem. Soc., 86, 3714 (1964);
12. c) S. L. Bearne and R. Wolfenden, J. Am. Chem. Soc., 117, 9588 (1995);
13. d) P. R. Andrews, G. D. Smith, and I. G. Young, Biochemistry, 12, 3492 (1973).
14. AMDase contains a number of hydrophobic amino acids, as shown in the primary structure in the previous paper. K. Miyamoto and H. Ohta, Appl. Microbiol. Biotech., 38, 234 (1992).
15. a) M. Nishio, Y. Umezawa, M. Hirota, and Y. Takeuchi, Tetrahedron, 51, 8665 (1995);
16. b) E. Tüchsen and C. Woodward, Biochemistry, 26, 1918 (1987);
17. c) S. K. Burley and G. A. Petsko, Science, 229, 23 (1985);
18. d) K. H. G. Verschueren, J. Kingma, H. J. Rozeboom, K. H. Kalk, D. B. Janssen, and B. W. Dijkstra, Biochemistry, 32, 9031 (1993).
19. G. A. Hall, Jr., and E. S. Hanrahan, J. Phys. Chem., 69, 2402 (1965).
20. a) D. Y. Jackson, M. N. Liang, P. A. Bartlett, and P. G. Schultz, Angew. Chem., Int. Ed. Engl., 31, 182 (1992);
21. b) D. Hilvert, S. H. Carpenter, K. D. Nared, and M-T. M. Auditor, Proc. Natl. Acad. Soc. U.S.A., 85, 4953 (1988);
22. c) U. H. Mortensen, S. J. Remington, and K. Breddam, Biochemistry, 33, 508 (1994).
23. Crucial roles of thiol ester formations in biology have recently been reported in the following papers.
24. a) J. T. Davis, R. N. Moore, B. Imperiali, A. J. Pratt, K. Kobayashi, S. Masamune, A. J. Sinskey, C. T. Walsh, T. Fukui, and K. Tomita, J. Biol. Chem., 262, 82 (1987);
25. b) W. Buckel and R. Keese, Angew. Chem., Int. Ed. Engl., 34, 1502 (1995);
26. c) A. W. Dodds, X.-D. Ren, A. C. Willis, and S. K. Alex Law, Nature, 379, 177 (1996).
27. -1.
28. E. C. Friedrich and D. B. Taggatt, J. Org. Chem., 40, 720 (1975).
29. J. H. Brewster and J. G. Buta, J. Am. Chem. Soc., 88, 2233 (1966).