17-Hydroxysteroid dehydrogenases of Mycobacterium sp. VKM Ac-1815D mutant strain.
Whole cells and crude extract of Mycobacterium sp. VKM Ac-1815D mutant strain Et1 were shown to carry out 17beta-reduction, 17beta-dehydrogenation and 1(2)-reduction of 3-keto-C(19)-steroids. Two 17-hydroxy steroid dehydrogenases (17-OH SDH) were partially purified from the strain by ammonium sulfate fractionation, ion-exchange chromatography on DEAE-sephacel and gel-filtration on Bio-Gel A. The enzymes differed in chromatographic properties and specific activities. One enzyme--17-OH SDH (2) (tetramer, M(r) approximately 210,000) was found to be responsible for bi-directional reduction-oxidation of steroids at C 17, whereas the other one--17-OH SDH (1) (monomer, M(r) approximately 68,000) specifically catalysed 17beta-dehydrogenation of 17-hydroxysteroids (testosterone and 1(2)-dehydro testosterone). The 17beta-reduction of 1-ene-17-ketosteroids was accompanied by 1(2)-reduction. A role of 1-ene-reductase as a steroid-binding protein associated with 17-OH SDH (2) in Mycobacterium sp. is discussed.
Egorova
O V
OV
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino State University, pr. Nauki 5, Pushchino, 142290 Moscow Region, Russia. vycherova@ibpm.serpukhov.su
Nikolayeva
V M
VM
Donova
M V
MV
D015067:17-Hydroxysteroid Dehydrogenases / Q000737:chemistry*; D000645:Ammonium Sulfate / Q000494:pharmacology; D001671:Biochemistry / Q000379:methods; D002384:Catalysis; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008956:Models, Chemical; D009154:Mutation; D009161:Mycobacterium / Q000201:enzymology* / Q000235:genetics; D010084:Oxidation-Reduction; D011485:Protein Binding; D013256:Steroids / Q000378:metabolism
D013256:Steroids; D015067:17-Hydroxysteroid Dehydrogenases; D000645:Ammonium Sulfate