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[微生物甾体转化酶。十一。不透明诺卡氏菌甾体-1-脱氢酶脱氢反应的可逆性]

[Steroid-transforming enzymes from microorganisms. XI. Reversibility of the dehydrogenation reaction of the steroid-1-dehydrogenase from Nocardia opaca].

作者信息

Groh H, Komel R, Deppmeyer V, Atrat P, Hörhold C

出版信息

Z Allg Mikrobiol. 1979;19(10):727-30.

PMID:44773
Abstract

Highly purified preparations of the 4-en-3-oxosteroid: (acceptor)-1-en-oxidoreductase from Nocardia opaca have been investigated in both types of reactions: 1.2-dehydrogenation of the 4-en-3-oxo-derivative and 1.2-hydrogenation of the 1.4-dien-3-oxo-derivative. It was not possible to separate the hydrogenating activity from the dehydrogenating activity by affinity chromatography, disc electrophoresis, SDS-electrophoresis, and isoelectric focusing techniques. The pure enzyme preparation is discussed as only one FAD depending protein acting in response to the system as a dehydrogenase as well as a reductase.

摘要

对来自不透明诺卡氏菌的高度纯化的4-烯-3-氧代类固醇:(受体)-1-烯氧化还原酶制剂进行了两种反应的研究:1. 4-烯-3-氧代衍生物的1,2-脱氢反应和2. 1,4-二烯-3-氧代衍生物的1,2-氢化反应。通过亲和色谱、圆盘电泳、SDS电泳和等电聚焦技术,无法将氢化活性与脱氢活性分离。该纯酶制剂被认为是仅一种依赖黄素腺嘌呤二核苷酸(FAD)的蛋白质,在该系统中既作为脱氢酶又作为还原酶起作用。

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