RGD Reference Report - Peroxisomal beta-oxidation of 2-methyl-branched acyl-CoA esters: stereospecific recognition of the 2S-methyl compounds by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase. - Rat Genome Database

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Peroxisomal beta-oxidation of 2-methyl-branched acyl-CoA esters: stereospecific recognition of the 2S-methyl compounds by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase.

Authors: Van Veldhoven, PP  Croes, K  Asselberghs, S  Herdewijn, P  Mannaerts, GP 
Citation: Van Veldhoven PP, etal., FEBS Lett. 1996 Jun 10;388(1):80-4.
RGD ID: 2299971
Pubmed: (View Article at PubMed) PMID:8654595

Trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase, purified from rat liver, both catalyse the desaturation of 2-methyl-branched acyl-CoAs. Upon incubation with the pure isomers of 2-methylpentadecanoyl-CoA, both enzymes acted only on the S-isomer. The R-isomer inhibited trihydroxycoprostanoyl-CoA oxidase but did not affect pristanoyl-CoA oxidase. The activity of both enzymes was suppressed by 3-methylheptadecanoyl-CoA. Valproyl-CoA and 2-ethylhexanoyl-CoA, however, did not influence the oxidases. Although only one isomer of 25R,S-trihydroxycoprostanovl-CoA was desaturated by trihydroxycoprostanoyl-CoA oxidase, isolated peroxisomes were able to act on both isomers, suggesting the presence of a racemase in these organelles. Given the opposite stereoselectivity of the 26-cholesterol hydroxylase and of the oxidase, the racemase is essential for bile acid formation.



Gene Ontology Annotations    

Biological Process

Cellular Component
peroxisome  (IDA)

Objects Annotated

Genes (Rattus norvegicus)
Acox2  (acyl-CoA oxidase 2)
Acox3  (acyl-CoA oxidase 3, pristanoyl)


Additional Information