Kinetics and thermodynamics of diacetyl reduction with NADPH by alpha-dicarbonyl reductase from pigeon liver.
alpha-dicarbonyl reductase from pigeon liver catalyzes diacetyl reduction with NADPH via an ordered Bi-Bi mechanism in which the coenzyme is the leading substrate, as deduced from the inhibition pattern by products and by acetone. The activation energy of the reaction has been calculated as 16.6 kcal/mol, delta H and delta F as 15.6 and 15.3 kcal/mol, respectively, and delta S as 1 cal/mol per k. Kinetic constants obtained for substrates (KmNADPH = 15 microM, KsNADPH = 10 microM; Kmdiacetyl = 0.5 mM, Ksdiacetyl = 0.35 mM) and products (KiNADP 50 microM; Kiacetoin = 100 mM) are about 10 times lower than those reported for this enzyme in the reduction of diacetyl with NADH. This confirms that NADPH is its physiological coenzyme.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D002074:Butanones / Q000378:metabolism*; D010856:Columbidae; D003931:Diacetyl / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009249:NADP / Q000378:metabolism*; D010084:Oxidation-Reduction; D013816:Thermodynamics
D002074:Butanones; D009249:NADP; D000429:Alcohol Oxidoreductases; C031043:L-glycol dehydrogenase; D003931:Diacetyl