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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Smeland TE,Li JX,Chu CH,Cuebas D,Schulz Hdoi
10.1016/s0006-291x(89)80098-1subject
Has Abstractpub_date
1989-05-15 00:00:00pages
988-92issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(89)80098-1journal_volume
160pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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journal_title:Biochemical and biophysical research communications
pub_type: 杂志文章
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