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
書誌事項
- タイトル別名
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- 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.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 20 (3), 295-297, 1997
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390001204621362560
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- NII論文ID
- 110003639044
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- NII書誌ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 4163698
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- PubMed
- 9084892
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- 本文言語コード
- en
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- JaLC
- NDL
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- PubMed
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