The isolation of acyl-CoA derivatives as products of partial reactions in the microsomal chain elongation of fatty acids.
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.
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D005227:Fatty Acids / Q000378:metabolism*; D006900:Hydroxylation; D066298:In Vitro Techniques; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D010171:Palmitoyl Coenzyme A / Q000378:metabolism; D051381:Rats
D000214:Acyl Coenzyme A; D005227:Fatty Acids; D010171:Palmitoyl Coenzyme A; D009249:NADP