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.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D006641:Histidinol; D007700:Kinetics; D008956:Models, Chemical; D009243:NAD; D012486:Salmonella typhimurium / Q000201:enzymology
D009243:NAD; D006641:Histidinol; D000429:Alcohol Oxidoreductases