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- W2051265684 abstract "The kinetic mechanism of α-acetohydroxy acid isomeroreductase from Salmonella typhimurium has been investigated by initial velocity kinetic and product inhibition studies. The results of the initial velocity studies are consistent with a sequential reaction. The product inhibition studies suggest an ordered reaction with NADPH and the acetohydroxy acid adding in that order, and dihydroxy acid release before NADP release. NADPH binding has been studied both by fluorimetric techniques and difference spectroscopy. From these investigations it has been calculated that 4 moles of NADPH bind per mole of enzyme; the first molecule of NADPH binds with a dissociation constant of 1.7 × 10−6m, the subsequent 3 moles of NADPH bind with a constant of 6 × 10−6m. Biphasic kinetics have been demonstrated at a wide range of NADPH concentrations. The occurrence of biphasic kinetics and two separate binding constants are discussed in terms of negative cooperativity." @default.
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- W2051265684 title "A kinetic study of α-acetohydroxy acid isomeroreductase from Salmonella typhimurium" @default.
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- W2051265684 doi "https://doi.org/10.1016/0003-9861(73)90605-x" @default.
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