Prokaryotic 20 beta-hydroxysteroid dehydrogenase is an enzyme of the 'short-chain, non-metalloenzyme' alcohol dehydrogenase type.
FEBS Lett
; 266(1-2): 51-4, 1990 Jun 18.
Article
en En
| MEDLINE
| ID: mdl-2194840
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.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Streptomyces
/
Cortisona Reductasa
/
20-Hidroxiesteroide Deshidrogenasas
Idioma:
En
Revista:
FEBS Lett
Año:
1990
Tipo del documento:
Article
País de afiliación:
Suecia