作者: Alfred W. Alberts , Robert M. Bell , P. Roy Vagelos
DOI: 10.1016/S0021-9258(19)45231-9
关键词:
摘要: β-Ketoacyl-acyl carrier protein (ACP) synthetase catalyzes the chain elongation step of fatty acid biosynthesis, condensation acyl-ACP with malonyl-ACP yielding β-ketoacyl-ACP, CO2, and ACP. This enzyme two additional reactions, acyl-CoA-ACP transacylation decarboxylation to form acetyl-ACP CO2. Both β-ketoacyl-ACP transacylase reactions are inhibited by low levels iodoacetamide, this inhibition can be prevented a prior incubation acyl-CoA compounds that substrates in reaction. These experiments suggest may have common site on enzyme. The decarboxylase reaction is only partially iodoacetamide. findings presented help explain acyl-CoA-dependent malonyl-CoA-14CO2 exchange catalyzed synthetase.