1997年3月
Stereospecific formation of (24R,25R)-3 alpha,7 alpha,12 alpha,24-tetrahydroxy-5 beta-cholestan-26-oic acid catalyzed with a peroxisomal bifunctional D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase
BIOLOGICAL & PHARMACEUTICAL BULLETIN
- ,
- ,
- ,
- ,
- ,
- 巻
- 20
- 号
- 3
- 開始ページ
- 295
- 終了ページ
- 297
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1248/bpb.20.295
- 出版者・発行元
- PHARMACEUTICAL SOC JAPAN
The absolute configuration of 3 alpha,7 alpha, 12 alpha,24-tetrahydroxy-5 beta-cholestan-26-oic acid CoA ester (V-CoA) produced by the incubation of (24E)-3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-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.
- リンク情報
-
- DOI
- https://doi.org/10.1248/bpb.20.295
- CiNii Articles
- http://ci.nii.ac.jp/naid/110003639044
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/9084892
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1997WP23000018&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1248/bpb.20.295
- ISSN : 0918-6158
- CiNii Articles ID : 110003639044
- PubMed ID : 9084892
- Web of Science ID : WOS:A1997WP23000018