Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases

Journal of Biological Chemistry

Volumn 274, Issue 23, 1999, Pages 16563-16568

  Nakajima, Keiji ^a   Kato, Hiroaki ^b   Oda, Jun'ichi ^c   Yamada, Yasuyuki ^a   Hashimoto, Takashi ^a  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c FUKUI PREFECTURAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

OXIDOREDUCTASE; TROPINONE REDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; STEREOSPECIFICITY;

ALCOHOL OXIDOREDUCTASES; AMINO ACID SEQUENCE; BINDING SITES; CATALYSIS; ESCHERICHIA COLI; HISTIDINE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; STEREOISOMERISM;

EID: 0033523086     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.23.16563     Document Type: Article

References (17)

1. Leete, E. (1990) Planta Med. 56, 339-352
2. Yamada, Y., Hashimoto, T., Endo, T., Yukimune, Y., Kohno, J., Hamaguchi, N., and Dräger, B. (1990) in Secondary Products from Plant Tissue Culture (Charlwood, B. V., and Rhodes, M. J. C., eds) pp. 227-242, Clarendon Press, Oxford
3. Nakajima, K., Hashimoto, T., and Yamada, Y. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 9591-9595
4. Nakajima, K., Hashimoto, T., and Yamada, Y. (1993) Plant Physiol. (Bethesda) 103, 1465-1466
5. Nakajima, K., Hashimoto, T., and Yamada, Y. (1994) J. Biol. Chem. 269, 11695-11698
6. Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzàlez-Duarte, R., Jeffery, J., and Ghosh, D. (1995) Biochemistry 34, 6003-6013
7. Nakajima, K., Yamashita, A., Akama, H., Nakatsu, T., Kato, H., Hashimoto, T., Oda, J., and Yamada, Y. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 4876-4881
8. Clackson, T., Güssow, D., and Jones, P. T. (1991) in PCR, A Practical Approach (McPherson, M. J., Quirke, P., and Taylor, G. R., eds) pp. 207-209, Oxford University Press, Oxford
9. Hashimoto, T., Nakajima, K., Ongena, G., and Yamada, Y. (1992) Plant Physiol. (Bethesda) 100, 836-845
10. Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Methods Enzymol. 185, 60-89
11. Portsteffen, A., Dräger, B., and Nahrstedt, A. (1994) Phytochemistry 37, 391-400
12. Fersht, A. (1985) Enzyme Structure and Mechanism, 2nd Ed., pp. 155-175, W. H. Freeman and Co., New York
13. Dräger, B., Funck, C., Höhler, A., Mrachatz, G., Nahrstedt, A., Portsteffen, A., Schaal, A., and Schmidt, R. (1994) Plant Cell Tissue Org. Cult. 38, 235-240
14. Molyneux, R., Pan, Y. T., Goldmann, A., Tepfer, D. A., and Elbein, A. (1993) Arch. Biochem. Biophys. 304, 81-88
15. Tepfer, D., Goldmann, A., Pamboukdjian, N., Maille, M., Lepingle, A., Chevalier, D., Dénarié, J., and Rosenberg, C. (1988) J. Bacteriol. 170, 1153-1161
16. Dräger, B., Almsick, A. V., and Mrachatz, G. (1995) Planta Med. 61, 577-579
17. Asano, N., Kato, A., Matsui, K., Walton, A. A., Nash, R. J., Molyneux, R. J., Hackett, L., Topping, J., and Winchester, B. (1997) Glycobiology 7, 1085-1088