Prokaryotic 20 beta-hydroxysteroid dehydrogenase is an enzyme of the 'short-chain, non-metalloenzyme' alcohol dehydrogenase type.
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.
Marekov
L
L
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Krook
M
M
Jörnvall
H
H
D015089:20-Hydroxysteroid Dehydrogenases / Q000032:analysis*; D000429:Alcohol Oxidoreductases / Q000145:classification; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D003349:Cortisone Reductase / Q000032:analysis* / Q000145:classification / Q000302:isolation & purification; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000201:enzymology*
D000596:Amino Acids; D000429:Alcohol Oxidoreductases; D015089:20-Hydroxysteroid Dehydrogenases; D003349:Cortisone Reductase