PURIFICATION AND SUBSTRATE SPECIFICITIES OF BACTERIAL HYDROXYSTEROID DEHYDROGENASES

被引：18

作者：

ROE, CR

KAPLAN, NO

机构：

[1] Department of Biochemistry, Brandeis University, Waltham

[2] Department of Chemistry, University of California, San Diego, La Jolla

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 12期

关键词：

D O I：

10.1021/bi00840a063

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Four highly specific hydroxysteroid dehydrogenases have been purified from bacteria. Substrate specificity studies reveal them to be (a) ring A/B trans 3β-hydroxysteroid dehydrogenase, (b) 3α-hydroxysteroid dehydrogenase unable to oxidize 3α-hydroxysteroids ring A/B cis with an 11-keto group, (c) ring A/B trans 3α-hydroxysteroid dehydrogenase, and (d) an axial 3-hydroxysteroid dehydrogenase. The possible application of these enzymes for the quantitative determination of specific steroid groups is presented. © 1969, American Chemical Society. All rights reserved.

引用

页码：5093 / &

共 17 条

[1] PURIFICATION AND PROPERTIES OF A 3ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM PSEUDOMONAS TESTOSTERONI [J].