PROKARYOTIC 20-BETA-HYDROXYSTEROID DEHYDROGENASE IS AN ENZYME OF THE SHORT-CHAIN, NONMETALLOENZYME ALCOHOL-DEHYDROGENASE TYPE

被引：77

作者：

MAREKOV, L ^{[1
]}

KROOK, M ^{[1
]}

JORNVALL, H ^{[1
]}

机构：

[1] KAROLINSKA INST,DEPT CHEM 1,S-10401 STOCKHOLM 60,SWEDEN

来源：

FEBS LETTERS | 1990年 / 266卷 / 1-2期

关键词：

Alcohol dehydrogenase; Amino acid sequence; Homology; Protein family; Steroid dehydrogenase; Tyrosine residue;

D O I：

10.1016/0014-5793(90)81504-H

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：

The primary structure of 20β-hydroxysteroid dehydrogenase from Streptomyces hydrogenans was determined after FPLC purification of a commercial preparation. Peptides obtained from different proteolytic cleavages were purified by reverse phase HPLC. The 255-residue structure deduced was found to be distantly homologous to those of Drosophila alcohol dehydrogenase and several other dehydrogenases, establishing that prokaryotic 20β-hydroxysteroid dehydrogenase as a member of the 'short-chain alcohol dehydrogenase family'. With the enzymes characterized, the identity is greatest (31-34%) towards 4 other prokaryotic dehydrogenases, but the family also includes mammalian steroid and prostaglandin dehydrogenases. These enzymes are low in Cys and have a strictly conserved Tyr residue that appears to be important. © 1990.

引用

页码：51 / 54

页数：4

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