Horse-liver alcohol dehydrogenase and Pseudomonas testosteroni 3(17)beta-hydroxysteroid dehydrogenase transfer epimeric hydrogens from NADH to 17beta-hydroxy-5alpha-androstan-3-one. An exception to one of the Alworth-Bentley rules.
In the reduction of 17beta-hydroxy-5alpha-androstan-3-one to the 3beta-alcohol, horse liver alcohol dehydrogenase utilizes the 4-pro-R hydrogen of NADH whereas the 3(17)beta-hydroxysteroid dehydrogenase of Pseudomonas testosteroni utulized the 4-pro-S hydrogen. These observations provide an exception to the rule proposed by Alworth and Bentley that with regard to the paired methylene hydrogens at C-4 of NADH and NADPH "the stereospecificity of a particular reaction is fixed and does not vary with the source of the enzyme preparation". It is also apparent that for these two enzymes, the selection of the side of NADH from which hydride is transferred to substrate cannot in both cases be dictated by the "best fit" of substrate and cofactor.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D013196:Dihydrotestosterone; D006736:Horses; D006913:Hydroxysteroid Dehydrogenases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D009243:NAD; D011549:Pseudomonas / Q000201:enzymology*; D013329:Structure-Activity Relationship
D013196:Dihydrotestosterone; D009243:NAD; D000429:Alcohol Oxidoreductases; D006913:Hydroxysteroid Dehydrogenases