Aragozzini F, Canzi E, Ferrari A, Maconi E, Sidjimov A
Biochem J. 1985 Sep 1;230(2):451-5. doi: 10.1042/bj2300451.
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.
在3α,7α-二羟基-[2,2,4,4-2H4]-、3α,7α-二羟基-[3β-2H]-和3β,7α-二羟基-[3α-2H]-5β-胆烷酸转化过程中,研究了产气荚膜梭菌使鹅去氧胆酸发生3-羟基差向异构化的机制。我们的研究结果排除了脱水-再水化途径,与以3-氧代鹅去氧胆酸为中间体的氧化还原机制相符。