Stereospecific Formation of(24R,25R)-3α,7α,12α,24-Tetrahydroxy-5β-cholestan-26-oic Acid Catalyzed with a Peroxisomal Bifunctional D-3-Hydroxyacyl-CoA Dehydratase/D-3-Hydroxyacyl-CoA Dehydrogenase

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タイトル別名
  • Stereospecific Formation fo (24R, 25R)-3.ALPHA., 7.ALPHA., 12.ALPHA., 24-Tetrahydroxy-5.BETA.-cholestan-26-oic Acid Catalyzed with a Paroxisomal Bifunctional D-3-Hydroxyacyl-CoA Dehydratase/D-3-Hydroxyacyl-CoA Dehydroge-nase.
  • Stereospecific Formation of 24R 25R 3アル

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The absolute configuration of 3α, 7α, 12α, 24-tetrahydroxy-5β-cholestan-26-oic acid CoA ester (V-CoA) produced by the incubation of (24E)-3α, 7α, 12α-trihydroxy-5β-cholest-24-en-26-oic acid CoA ester (24E-THC-CoA) with D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase (D-bifunctional protein) was investigated. When 24E-THC-CoA was incubated with D-bifunctional protein the formation of only one isomer (24R, 25R-isomer) of four possible stereoisomers of V-CoA was observed, which suggested the cis-addition of water to a side chain double bond of 24E-THC-CoA. The dehydration reaction of V-CoA catalyzed by D-bifunctional protein was also observed when (24R, 25R)-V-CoA was used as a substrate. The other three isomers (24R, 25S-, 24S, 25R- and 24S, 25S-isomers) were not dehydrated with D-bifunctional protein. These results showed that D-bifunctional protein catalyzes stereospecifically the hydration and dehydration step in bile acid biosynthesis.

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