Substrate Stereospecificity in Oxidation of (25S)-3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA by Peroxisomal Trihydroxy-5β- cholestanoyl-CoA Oxidase

Partly purified 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase from rabbit liver peroxisomes was found to convert the 25S- but not the 25R diastereoisomer of 3α,7α,12α-trihydroxy-5β-cholestan-27-oyl-CoA into (24E)-3α,7α,12α-trihydroxy-5β-cholest-24-en-27-oic acid. In the presence of a peroxisomal...

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Published inBiochemical and biophysical research communications Vol. 224; no. 1; pp. 37 - 42
Main Authors Pedersen, Jan I., Veggan, Turid, Björkhem, Ingemar
Format Journal Article
LanguageEnglish
Published Elsevier Inc 05.07.1996
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Summary:Partly purified 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase from rabbit liver peroxisomes was found to convert the 25S- but not the 25R diastereoisomer of 3α,7α,12α-trihydroxy-5β-cholestan-27-oyl-CoA into (24E)-3α,7α,12α-trihydroxy-5β-cholest-24-en-27-oic acid. In the presence of a peroxisomal THCA-CoA racemase, however, also the 25R isomer was oxidized. Since the mitochondrial steroid-27-hydroxylase, responsible for formation of THCA, is 25R specific a racemase seems to be obligatory for formation of cholic acid by the normal peroxisomal-dependent pathway.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.0981