Steady-state investigations of the mechanism of histidinol dehydrogenase.

ABSTRACT: 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.

SUBMITTER: Gorisch H 

PROVIDER: S-EPMC1161136 | biostudies-other | 1979 Jul

REPOSITORIES: biostudies-other