来自大肠杆菌的7α-羟基类固醇脱氢酶的特异性
The specificity of a 7 alpha-hydroxy steroid dehydrogenase from Escherichia coli.
作者信息
Haslewood E S, Haslewood G A
出版信息
Biochem J. 1976 Jul 1;157(1):207-10. doi: 10.1042/bj1570207.
Abstract
- Thirty-eight steroids were tested as substrates for a 7 alpha-hydroxy steroid dehydrogenase preparation from a strain of Escherichia coli; an improved method of making the crude enzyme is described. 2. Steroids having a 7 alpha-hydroxyl group in the molecule were substrates except (a) when the 5 beta-cholan-24-oic acid side chain was shortened to less than four carbon atoms and (b) in certain cases when sulphate ester groups were present in the molecule. 3. For testing with the enzyme, a new specimen of 7 alpha-hydroxy-3,12-dioxo-5 beta-cholan-24-oic acid was made, which had properties different from those previously described.
摘要
- 对38种甾体进行了测试，以作为来自大肠杆菌菌株的7α-羟基甾体脱氢酶制剂的底物；描述了一种制备粗酶的改进方法。2. 分子中具有7α-羟基的甾体是底物，但有以下例外情况：(a) 当5β-胆烷-24-酸侧链缩短至少于四个碳原子时；(b) 在分子中存在硫酸酯基团的某些情况下。3. 为了用该酶进行测试，制备了一种新的7α-羟基-3,12-二氧代-5β-胆烷-24-酸样品，其性质与先前描述的不同。
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