Mutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B

Journal of Bacteriology

Volumn 179, Issue 24, 1997, Pages 7742-7747

  Kim, Suhng Wook ^a   Joo, Soyoung ^a   Choi, Gildon ^a   Cho, Hyun Soo ^a   Oh, Byung Ha ^a   Choi, Kwan Yong ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ALANINE; ASPARAGINE; ASPARTIC ACID; CYSTEINE; EQUILENIN; STEROID DELTA ISOMERASE; THIOL DERIVATIVE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; GENE MUTATION; HYDROGEN BOND; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

FELIS CATUS; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0001033697     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.24.7742-7747.1997     Document Type: Article

References (37)

1. 5-3-ketosteroid isomerase probed by site-directed mutagenesis and UV resonance raman-spectroscopy. Protein Sci. 1:259-270.
2. 5-3-ketosteroid isomerase revisited: substrate polarization by active-site residues. Biochemistry 34:4441-4447.
3. 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.
4. 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: kinetic properties of a modified enzyme in which tyrosine 14 is replaced by 3-fluorotyrosine. Biochemistry 33:2682-2687.
5. 5-3-ketosteroid isomerase from Pseudomonas testosteroni. Gene 58:257-264.
6. Collier, H. B. 1973. A note on the molar absorptivity of reduced Ellman's reagent, 3-carboxylato-4-nitrothiophenolate. Anal. Biochem. 56:310-311.
7. Copeland, R. A. 1993. Methods of protein analysis: a practical guide to laboratory protocols. Chapman and Hall, New York, N.Y.
8. Ellman, G. L. 1959. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82: 70-71.
9. Gerlt, J. A., and P. G. Gassman. 1993. An explanation for rapid enzyme-catalyzed proton abstraction from carbon acids: importance of late transition states in concerted mechanisms. J. Am. Chem. Soc. 115:11552-11568.
10. Gerlt, J. A., and P. G. Gassman. 1993. Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyltransfer reactions, and displacement reactions of phosphodiesters. Biochemistry 32:11943-11952.
11. Gerlt, J. A., J. W. Kozarich, G. L. Kenyon, and P. G. Gassman. 1991. Electrophilic catalysis can explain the unexpected acidity of carbon acids in enzyme-catalyzed reactions. J. Am. Chem. Soc. 113:9667-9669.
12. 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: site-specific replacement of the active site base, aspartate 38, by the weaker base alanine-3-sulfinate. Biochemistry 33:2672-2681.
13. 5-3-ketosteroid isomerase as revealed by site-directed mutagenesis of the catalytic base aspartate-38. Biochemistry 34:14245-14253.
14. 5-3-ketosteroid isomerase from Pseudomonas putida biotype B. J. Bacteriol. 177:2602-2605.
15. 5-3-ketosteroid isomerase from Pseudomonas putida biotype B. J. Bacteriol. 176:6672-6676.
16. Kim, S. W., S.-S. Cha, H.-S. Cho, J.-S. Kim, N.-C. Ha, M.-J. Cho, S. Joo, K.-K. Kim, K. Y. Choi, and B.-H. Oh. Biochemistry, in press.
17. Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24:946-950.
18. 5-3-ketosteroid isomerase. Biochemistry 28:149-159.
19. 5-3-ketosteroid isomerase by combined kinetic, magnetic resonance, and X-ray diffraction methods. Biochemistry 26:3927-3937.
20. Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
21. 5-3-oxosteroid isomerase from Pseudomonas putida biotype B. J. Biol. Chem. 261:6454-6460.
22. Oh, B.-H., S. W. Kim, S.-E. Ryu, S.-S. Kim, M.-K. Yoon, and K. Y. Choi. 1996. Crystallization and preliminary x-ray crystallographic studies of ketosteroid isomerase from Pseudomonas putida biotype B. Proteins 24:514-515.
23. Pollack, R. M., P. L. Bounds, and C. L. Bevins. 1989. Chemical and enzymatic conversion of β, γ-enones to α, β-enones, p. 559-597. In S. Patai and Z. Rappoport (ed.), The chemistry of enones. John Wiley and Sons Ltd., New York, N.Y.
24. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
25. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
26. Schwab, J. M., and B. S. Henderson. 1990. Enzyme-catalyzed allylic rearrangements. Chem. Rev. 90:1203-1245.
27. 5-3-ketosteroid isomerase from Pseudomonas putida dependent on 1,4,6-androstatrien-3-one-17β-o1. J. Biol. Chem. 255:2690-2693.
28. Tamaoka, J., D.-M. Ha, and K. Komagata. 1987. Reclassification of Pseudomonas acidovorans den Dooren de Jong 1926 and Pseudomonas testosteroni Marcus and Talalay 1956 as Comamonas acidovorans comb. nov. and Comamonas testosteroni comb. nov., with an emended description of the genus Comamonas. Int. J. Syst. Bacteriol. 37:52-59.
29. 5-3-ketosteroid isomerase. Architecture and location of the active center. J. Biol. Chem. 259:9096-9103.
30. 5-steroid isomerase. Science 276:415-418.
31. 5-3-ketosteroid isomerase. Direct spectroscopic evidence for dienol intermediates. Biochemistry 30:4991-4997.
32. 5-3-ketosteroid isomerase by kinetic deuterium isotope effects. Biochemistry 30:10858-10865.
33. 5-steroid isomerase by mutation of the catalytic base (Asp-38 to Glu-38). J. Am. Chem. Soc. 13:5890-5892.
34. 5-3-ketosteroid isomerase. Biochemistry 34:426-434.
35. 5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids. Biochemistry 36:3458-3472.
36. 5-3-ketosteroid isomerase. Proc. Natl. Acad. Sci. USA 93:8220-8224.
37. 5-3-ketosteroid isomerase by steroid binding. Biochemistry 34:6562-6572.