A study on the mechanism of the epimerization at C-3 of chenodeoxycholic acid by Clostridium perfringens.
The mechanism of 3-hydroxy epimerization of chenodeoxycholic acid by Clostridium perfringens was investigated in 3 alpha, 7 alpha-dihydroxy-[2,2,4,4-2H4]-, 3 alpha, 7 alpha-dihydroxy-[3 beta-2H]- and 3 beta, 7 alpha-dihydroxy-[3 alpha-2H]-5 beta-cholanoic acid transformations. Our findings rule out a dehydration-rehydration pathway and agree with a redox mechanism involving 3-oxochenodeoxycholic acid as intermediate.
Aragozzini
F
F
Canzi
E
E
Ferrari
A
A
Maconi
E
E
Sidjimov
A
A
D001647:Bile Acids and Salts / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002635:Chenodeoxycholic Acid / Q000378:metabolism*; D003016:Clostridium perfringens / Q000378:metabolism*; D003903:Deuterium; D010084:Oxidation-Reduction; D013237:Stereoisomerism
D001647:Bile Acids and Salts; D002635:Chenodeoxycholic Acid; D003903:Deuterium