The 3-hydroxyacyl-CoA epimerase activity of rat liver peroxisomes is due to the combined actions of two enoyl-CoA hydratases: a revision of the epimerase-dependent pathway of unsaturated fatty acid oxidation.

Abstract:

:Chromatography of a rat liver extract on DEAE-cellulose resulted in the near total loss of 3-hydroxyacyl-CoA epimerase activity. The activity was regained either when fractions were recombined or when purified crotonase was added to the early column fractions. A new enoyl-CoA hydratase present in these early fractions catalyzes the conversion of D-3-hydroxyacyl-CoA to 2-trans-enoyl-CoA which can be hydrated by crotonase or the peroxisomal bifunctional enzyme to L-3-hydroxyacyl-CoA. Thus, the 3-hydroxyacyl-CoA epimerase activity is due to the combined actions of two enoyl-CoA hydratases with opposite stereospecificities.

authors

Smeland TE,Li JX,Chu CH,Cuebas D,Schulz H

doi

10.1016/s0006-291x(89)80098-1

subject

Has Abstract

pub_date

1989-05-15 00:00:00

pages

988-92

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(89)80098-1

journal_volume

160

pub_type

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