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- W2009969183 abstract "Acetolactate nonenzymatically reduced flavins, quinones and nicotinamide coenzymes in a time-dependent manner at physiological pH and moderate temperature. In the presence of excess acetolactate, the reduction of FAD and NAD+ followed pseudo-first-order kinetics. The rate of reduction was proportional to the concentration of acetolactate, and the rate constants at 37°C and pH 7.5 were 4.8 · 10−2 M−1 s−1 and 7.4 · 10−3 M−1 s−1 for FAD and NAD+, respectively. In contrast, ubiquinone reduction followed pseudo-zero-order kinetics in the presence of excess acetolactate. At 37°C and pH 7.5, the rate of reduction was proportional to the acetolactate concentration, and the apparent rate constant was 8.3 · 10−6 s−1. In contrast to FAD, the rate of reduction of ubiquinone was higher at low pH. The kinetics of ubiquinone reduction suggested that the rate-limiting step was acetolactate decarboxylation and formation of the enolate anion, whereas the rate of FAD reduction was governed by the second-order reaction of the enolate anion. Following the oxidation, acetolactate was converted to diacetyl. Reduced FAD formed by the reaction with acetolactate generated a low rate of O2 consumption during assays of the oxygenase activity of acetohydroxy acid synthase. The reaction of acetolactate with quinones may provide a mechanism for the nonenzymatic formation diacetyl in whole milk." @default.
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- W2009969183 date "1995-12-01" @default.
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- W2009969183 title "Nonenzymatic acetolactate oxidation to diacetyl by flavin, nicotinamide and quinone coenzymes" @default.
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- W2009969183 doi "https://doi.org/10.1016/0304-4165(95)00103-4" @default.
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