Prokaryotic 20 beta-hydroxysteroid dehydrogenase is an enzyme of the 'short-chain, non-metalloenzyme' alcohol dehydrogenase type.

Abstract:

:The primary structure of 20 beta-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 20 beta-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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Marekov L,Krook M,Jörnvall H

doi

10.1016/0014-5793(90)81504-h

subject

Has Abstract

pub_date

1990-06-18 00:00:00

pages

51-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)81504-H

journal_volume

266

pub_type

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