Steric Course of Reaction Catalyzed by the Enoyl Acyl‐Carrier‐Protein Reductase of Escherichia coli

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Abstract
The steric course of the reaction catalyzed by E. coli enoyl acyl-carrier-protein reductase (EC 1.3.1.9 and EC 1.3.1.10) was studied. trans-2-[2-2H1]Decenoic and trans-2-[3-2H1]decenoic acids were synthesized and converted to the corresponding decenoyl thiol esters with CoA or acyl carrier protein. These deuterium-labled decenoyl thiol esters were incubated with purified enoyl acyl-carrier-protein reductase in the presence of NADPH or NADH. The unlabeled trans-2-decenoyl thiol esters were incubated with enoyl acyl-carrier-protein reductase in the presence of (4S)-[4-2H1]NADH. The unlabeled decenoyl thiol esters were also incubated with the enzyme in 2H2O. The decanoic acids formed in the above incubations were extracted and subjected to the action of acyl-CoA oxidase, which had been previously shown to catalyze the anti-elimination of the pro-2R and pro-3R hydrogens of acyl-CoA. The resulting products, 2-decenoyl-CoA, were converted to methyl esters and their deuterium contents were analyzed by gas chromatography/mass spectrometry. The reduction catalyzed by E. coli enoyl acyl-carrier-protein reductase occurs by a syn addition of hydrogen via a 2-Re, 3-Si attack on the double bond.

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