Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity.
Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity.
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醛糖和醛还原酶表现出异皮质类固醇还原酶活性。
DOI：
10.1111/j.1432-1033.1983.tb07280.x
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Monder,C
中科院分区：
文献类型：
--
作者：
Wermuth,B;Monder,C
在本文中，我们描述了含有17β-羟醛侧链的皮质类固醇代谢物（异皮质类固醇）通过醛糖和醛还原酶从人体组织中还原。醛糖还原酶以大约相同的速率催化来自皮质醇和皮质酮的醛的还原，而醛还原酶优先作用于来自17-脱氧皮质类固醇的醛。在可比的减少率的米氏常数为最好的类固醇醛是一个数量级低于迄今为止最好的基板。我们提出，醛糖和醛还原酶通过Monder和Bradlow提出的“长环”途径[（1977）J. Steroid Biochem.8，897-908]，经由羟醛中间体参与皮质类固醇酮醇侧链向二醇侧链的转化。
In this paper we describe the reduction of corticosteroid metabolites containing the 17β‐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].