Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7α-hydroxysteroid dehydrogenase from Escherichia coli

Journal of Biochemistry

Volumn 124, Issue 3, 1998, Pages 634-641

  Tanabe, Tetsurou ^a   Tanaka, Nobutaka ^b   Uchikawa, Kouichiro ^a   Kabashima, Tsutomu ^a   Ito, Kiyoshi ^a   Nonaka, Takamasa ^c   Mitsui, Yukio ^c   Tsuru, Masato ^a   Yoshimoto, Tadashi ^a  

^a NAGASAKI UNIVERSITY   (Japan)

^b SHOWA UNIVERSITY   (Japan)

^c NAGAOKA UNIVERSITY OF TECHNOLOGY   (Japan)

Author keywords

Catalytic mechanism; Site directed mutagenesis; Steroid dehydrogenase; X ray analysis

Indexed keywords

BACTERIAL ENZYME; HYDROXYSTEROID DEHYDROGENASE; LYSINE; MUTANT PROTEIN; SERINE; TYROSINE;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FELIS CATUS;

EID: 0031716024     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022159     Document Type: Article

References (28)

1. MacDonald, I.A., Williams, C.N., and Mahony, D.E. (1973) 7α-Hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies. Biochim. Biophys. Acta 309, 243-253
2. Prebha, V., Gupta, M., Seiffge, D., and Gupta, K.G. (1990) Purification of 7α-hydroxysteroid dehydrogenase from Escherichia coli strain 080. Can. J. Microbiol. 36, 131-135
3. Yoshimoto, T., Higashi, H., Kanatani, K., Xu, S.L., Nagai, H., Oyama, H., Kurazono, K., and Tsuru, D. (1991) Cloning and sequencing of the 7α-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme. J. Bacteriol. 173, 2173-2179
4. Yoshimoto, T., Nagai., H., Ito, K., and Tsuru, D. (1993) Location of the 7α-hydroxysteroid dehydrogenase gene (hdhA) on the physical map of the Escherichia coli chromosome. J. Bacteriol. 175, 5730
5. Jörnvall, H., Bahr-Lindstrom, H., Jany, K.-D., Ulmer, W., and Froschle, M. (1995) Short-chain dehydrogenases/reductases. Biochemistry 34, 6003-6013
6. Tanaka, N., Nonaka, T., Tanabe, T., Yoshimoto, T., Tsuru, D., and Mitsui, Y. (1996) Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35, 7715-7730
7. Daws, T., Lim, C.-J., and Fuchs, J.A. (1989) In vitro construction of gshB::kan in Escherichia coli and use of gshB::kan in mapping the gshB locus. J. Bacteriol. 171, 5218-5221
8. Bingham, R.J., Hall, K.S., and Slonczewski, J.L. (1990) Alkaline induction of a novel gene locus, alx, in Escherichia coli. J. Bacteriol. 172, 2184-2186
9. Dower, W.J. (1988) High efficiency transformation of Escherichia coli by high voltage electroporation. Nucleic Acids Res. 16, 6127-6145
10. Birnboim, H.C. and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7, 1513-1523
11. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59
12. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
13. Stinson, R.A. and Holbrook, J.J. (1973) Equilibrium binding of nicotine amide nucleotides to lactate dehydrogenases. Biochem. J. 131, 719-728
14. Tanaka, N., Nonaka, T., Yoshimoto, T., Tsuru, D., and Mitsui, Y. (1996) Crystallization and preliminary X-ray crystallographic studies of 7α-hydroxysteroid dehydrogenase from Escherichia coli. Acta Crystallogr. D52, 215-217
15. Brünger, A.T. (1992) X-PLOR Version 3.1. A System for X-Ray Crystallograph and NMR, Yale University Press, New Haven, CT
16. Brünger, A.T. and Krukowski, A. (1990) Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr. A46, 585-593
17. Persson, B., Krook, M., and Jörnvall, H. (1991) Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200, 537-543
18. +-dependent 15-hydroxyprostaglandin dehydrogenase yields a catalytically inactive enzyme. Biochem. Biophys. Res. Commun. 176, 840-845
19. Albalat, R., Duarte, G., and Atrian, S. (1992) Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl group of Tyr152 is involved in the active site of the enzyme. FEBS Lett. 165, 190-196
20. Obeid, J. and White, P.C. (1992) Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Commun. 188, 222-227
21. Chen, Z., Jiang, J.C., Lin, Z.G., Lee, W.R., Baker, M.E., and Chang, S.H. (1993) Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry 32, 3342-3346
22. Cols, N., Marfany, G., Atrian, S., and Gonzalez-Duarte, R. (1993) Effect of site-directed mutagenesis on conserved positions of Drosophila alcohol dehydrogenase. FEBS Lett. 319, 90-94
23. Whitely, J.M., Xuong, N.H., and Varughese, K.I. (1993) in Chemistry and Biology of Pteridines and Folates (Ayling, J.E., Nair, M.G., and Baugh, C.M., eds.), pp. 115-121, Plenum, New York
24. Varughese, K.I., Skinner, M.M., Whiteley, J.M., Matthews, D.A., and Xuong, N.H. (1992) Crystal structure of rat liver dihydropteridine reductase. Proc. Natl. Acad. Sci. USA 89, 6080-6084
25. 3-Lys-containing family of reductases and dehydrogenases. Proc. Natl. Acad. Sci. USA 91, 5582-5586
26. Kiefer, P.M., Varughese, K.I., Su, Y., Xuong, N.-H., Chang, C.-F., Gupta, P., Bray, T., and Whiteley, J.M. (1996) Altered structural and mechanistic properties of mutant dihydropteridine reductases. J. Biol. Chem. 271, 3437-3444
27. Oppermann, C.T.U., Filling, C., Berndt, D.K., Persson, B., Benach, J., Ladenstein, R., and Jörnvall, H. (1997) Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/ reductase reactions. Biochemistry 36, 34-40
28. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950