Nonenzymatic acetolactate oxidation to diacetyl by flavin, nicotinamide and quinone coenzymes
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 proportio...
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Published in | Biochimica et biophysica acta Vol. 1245; no. 3; pp. 366 - 370 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
14.12.1995
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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 O
2 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. |
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AbstractList | 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 degrees C and pH 7.5 were 4.8 x 10(-2) M-1 s-1 and 7.4 x 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 degrees C and pH 7.5, the rate of reduction was proportional to the acetolactate concentration, and the apparent rate constant was 8.3 x 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. 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 O 2 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. |
Author | Whitman, William B. Park, Sang Ho Xing, Ruye |
Author_xml | – sequence: 1 givenname: Sang Ho surname: Park fullname: Park, Sang Ho – sequence: 2 givenname: Ruye surname: Xing fullname: Xing, Ruye – sequence: 3 givenname: William B. surname: Whitman fullname: Whitman, William B. email: whitman@bscr.uga.edu |
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Keywords | NAD reduction Flavin reduction Tricine Methanococcus Acetolactate AHAS Ubiquinone reduction Acetohydroxy acid synthase |
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Biotechnol. doi: 10.1007/BF00169412 contributor: fullname: Hugenholtz – volume: 59 start-page: 1838 year: 1993 ident: 10.1016/0304-4165(95)00103-4_BIB5 publication-title: Appl. Env. Microbiol. doi: 10.1128/AEM.59.6.1838-1841.1993 contributor: fullname: Romano |
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Snippet | Acetolactate nonenzymatically reduced flavins, quinones and nicotinamide coenzymes in a time-dependent manner at physiological pH and moderate temperature. In... |
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SubjectTerms | Acetohydroxy acid synthase Acetolactate Benzoquinones - metabolism Chromatography, Thin Layer Diacetyl - metabolism Flavin reduction Flavins - metabolism Lactates - metabolism Methanococcus NAD reduction Niacinamide - metabolism Oxidation-Reduction Ubiquinone reduction |
Title | Nonenzymatic acetolactate oxidation to diacetyl by flavin, nicotinamide and quinone coenzymes |
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