Mode of action of steroid desmolase and reductases synthesized by Clostridium 'scindens' (formerly Clostridium strain 19).

• Main Authors: J Winter, G N Morris, S O'Rourke-Locascio, V D Bokkenheuser, E H Mosbach, B I Cohen, P B Hylemon
• Format: Article
• Language: English
• Published: Elsevier 1984-10-01
• Series: Journal of Lipid Research
• Online Access: http://www.sciencedirect.com/science/article/pii/S0022227520377221

A recently isolated hitherto unknown Clostridium from human feces, designated Clostridium ''scindens'' (formerly strain 19), synthesizes at least two enzymes active on the side-chain of the steroid molecule and two enzymes active on the hydroxyl groups of the 7-position of bile acids. Steroid desmolase, responsible for side-chain cleavage of corticoids, and 20 alpha-hydroxysteroid dehydrogenase have not been detected in any other bacterial species of the resident colonic flora. Steroid desmolase is Eh-dependent (optimum ca. -130 mV), requires a hydroxy group at C-17, and preferably an alpha-ketol group in the side-chain; an alpha-hydroxy group at C-20 reduces and a beta-hydroxy group at C-20 prevents side-chain cleavage. With suitable substrates, the yield of C-19 steroids is proportional to the bacterial multiplication rate. 20 alpha-Hydroxysteroid dehydrogenase (20 alpha-HSDH) is also Eh-dependent (optimum ca. -300 mV) and reduces the C-20 keto function to an alpha-hydroxy group, regardless of the presence or absence of a hydroxy group at C-17. 7 alpha-Dehydroxylase metabolizes cholic and chenodeoxycholic acid, while 7 beta-hydroxysteroid dehydrogenase acts upon ursodeoxycholic acid. The latter two enzymes are not specific for C. scindens.