PMID: 37916Jun 21, 1979

The isolation of acyl-CoA derivatives as products of partial reactions in the microsomal chain elongation of fatty acids

Biochimica Et Biophysica Acta
J T Bernert, H Sprecher


An analysis of overall chain elongation, condensation, beta-hydroxyacyl-CoA dehydrase and 2-trans enoyl-CoA reductase reactions, using the appropriate CoA derivatives as substrates which are required in the microsomal chain elongation of both palmitoyl-CoA and 6,9-octadecadienoyl-CoA, demonstrated that in each instance, the products of these reactions were the CoA derivatives. Reverse dehydrase reactions run with 2-trans enoyl-CoA derivatives as substrates, in the absence of NADPH, revealed that the product was the beta-hydroxyacyl-Coa. In the presence of NADPH, incubations with beta-hydroxyacyl-CoA demonstrated that both the 2-trans derivatives and the alpha, beta-saturated product were recovered as their CoA derivatives. These latter findings are more consistent with the involvement of discrete dehydrase and 2-trans-enoyl-CoA reductase enzymes rather than a single protein catalyzing two reactions.


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Related Concepts

Acyl Coenzyme A
Saturated Fat
Microsomes, Liver
Palmitoyl Coenzyme A
Rats, Laboratory
In Vitro [Publication Type]

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