Prokaryotic 20β‐hydroxysteroid dehydrogenase is an enzyme of the ‘short‐chain, non‐metalloenzyme’ alcohol dehydrogenase type

FEBS Letters

Krook, Maria¹  Marekov, Lyuben¹  Jörnvall, Hans¹ 

[1] Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

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

DOI  :  10.1016/0014-5793(90)81504-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown