Wermuth B, Monder C
Eur J Biochem. 1983 Mar 15;131(2):423-6. doi: 10.1111/j.1432-1033.1983.tb07280.x.
In this paper we describe the reduction of corticosteroid metabolites containing the 17 beta-aldol side chain (isocorticosteroids) by aldose and aldehyde reductase from human tissues. Aldose reductase catalyzed the reduction of the aldehydes derived from cortisol and corticosterone at about the same rate, whereas aldehyde reductase preferentially acted on the aldehydes derived from 17-deoxycorticosteroids. At comparable rates of reduction the Michaelis constants for the best steroid aldehydes were one order of magnitude lower than for the hitherto best substrates. We propose that aldose and aldehyde reductase participate in the conversion of the corticosteroid ketol side chain to the glycol side chain via an aldol intermediate by the 'long loop' pathway proposed by Monder and Bradlow [(1977) J. Steroid Biochem. 8, 897-908].
在本文中，我们描述了人体组织中的醛糖还原酶和醛还原酶对含有17β - 羟醛侧链的皮质类固醇代谢物（异皮质类固醇）的还原作用。醛糖还原酶催化皮质醇和皮质酮衍生的醛的还原，速率大致相同，而醛还原酶则优先作用于17 - 脱氧皮质类固醇衍生的醛。在可比的还原速率下，最佳类固醇醛的米氏常数比迄今为止最佳底物的米氏常数低一个数量级。我们提出，醛糖还原酶和醛还原酶通过Monder和Bradlow [（1977年）《类固醇生物化学杂志》8卷，897 - 908页]提出的“长环”途径，通过醛醇中间体参与皮质类固醇酮醇侧链向二醇侧链的转化。
