Steady-state investigations of the mechanism of histidinol dehydrogenase.
Initial velocities of the histidinol dehydrogenase reaction (EC 1.1.1.23) were measured as a function of the concentrations of the substrates histidinol and NAD+ and in the presence and absence of the product NADH. The data are consistent with a Bi Uni Uni Bi Ping Pong mechanism. The kinetic constants of this mechanism were determined; Km for histidinol was found to be 14 microM and for NAD+ 0.7 mV; Ki for NAD+ was 0.4 mM.
7 references, click to expand
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The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.Biochim Biophys Acta. 1963 Jan 8;67:104-37 PMID: 14021667
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Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties.J Mol Biol. 1966 Dec 28;22(2):305-23 PMID: 5339687
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