Nishinaka T, Kinoshita Y, Terada N, Terada T, Mizoguchi T, Nishihara T
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Enzyme. 1992;46(4-5):221-8. doi: 10.1159/000468791.
Three enzyme forms (CR1, CR2 and CR3) of carbonyl reductase were purified from chicken liver with using 4-benzoylpyridine as a substrate. CR1 was a dimeric enzyme composed of two identical 25-kD subunits. CR2 and CR3 were monomeric enzymes whose molecular weights were both 32 kD. CR1 exhibited 17 beta-hydroxysteroid dehydrogenase activity as well as carbonyl reductase activity in the presence of both NADP(H) and NAD(H). CR2 and CR3 had similar properties with regard to substrate specificity and inhibitor sensitivity. They could exhibit the activity only with NADPH and had no hydroxysteroid dehydrogenase activity. CR2 and CR3 cross-reacted with anti-chicken kidney carbonyl reductase antibody, though CR1 did not. The results suggest that CR1 is a hydroxysteroid dehydrogenase, and CR2 and CR3 are similar to each other and to the kidney enzymes.
以4-苯甲酰吡啶为底物，从鸡肝中纯化出了羰基还原酶的三种酶形式（CR1、CR2和CR3）。CR1是一种二聚体酶，由两个相同的25-kD亚基组成。CR2和CR3是单体酶，分子量均为32 kD。在同时存在NADP(H)和NAD(H)的情况下，CR1表现出17β-羟基类固醇脱氢酶活性以及羰基还原酶活性。CR2和CR3在底物特异性和抑制剂敏感性方面具有相似的特性。它们仅在NADPH存在时才表现出活性，且没有羟基类固醇脱氢酶活性。CR2和CR3与抗鸡肾羰基还原酶抗体发生交叉反应，而CR1则不发生。结果表明，CR1是一种羟基类固醇脱氢酶，CR2和CR3彼此相似且与肾酶相似。
