Abstract
1. 1. The dependence of the beef liver diacetyl reductase (acetoin:NAD oxido-reductase, EC 1.1.1.5) reaction rate on the concentration of substrates and the product inhibition pattern are investigated at optimum pH. The Michaelis and dissociation constants for the reaction in the direction diacetyl→acetoin are evaluated. 2. 2. The results are consistent with the features of both a Theorell-Chance and a rapid equilibrium random Bi-Bi mechanism with two dead-end ternary complexes. However, it is concluded that the Theorell-Chance mechanism is the more probable one. 3. 3. Km values for diacetyl and NADH seem to indicate that the enzyme is operative under normal physiological conditions.
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