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 Lettjournal_title
FEBS lettersauthors
Marekov L,Krook M,Jörnvall Hdoi
10.1016/0014-5793(90)81504-hsubject
Has Abstractpub_date
1990-06-18 00:00:00pages
51-4issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)81504-Hjournal_volume
266pub_type
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