| Autor: |
Saito, Kazuki, Kawaguchi, Akihiko, Seyama, Yousuke, Yamakawa, Tamio, Okuda, Shigenobu |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 6/1/81, Vol. 116 Issue 3, p581-586, 6p |
| Abstrakt: |
The steric course of the reaction catalyzed by Escherichia coli enoyl acyl-carrier-protein reductase was studied. 1. 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-labeled decenoyl thiol esters were incubated with purified enoyl acyl-carrier-protein reductase in the presence of NADPH or NADH. 2. 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-CoAs, were converted to methyl esters and their deuterium contents were analyzed by gas chromatography/mass spectrometry. The results suggested that 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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