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Arch Biochem Biophys. 1983 Sep;225(2):621-9.

Human liver cytosolic malate dehydrogenase: purification, kinetic properties, and role in ethanol metabolism.


Cytosolic malate dehydrogenase from human liver was isolated and its physical and kinetic properties were determined. The enzyme had a molecular weight of 72,000 +/- 2000 and an amino acid composition similar to those of malate dehydrogenases from other species. The kinetic behaviour of the enzyme was consistent with an Ordered Bi Bi mechanism. The following values (microM) of the kinetic parameters were obtained at pH 7.4 and 37 degrees C: Ka, 17; Kia, 3.6; Kb, 51; Kib, 68; Kp, 770; Kip, 10,700; Kq, 42; Kiq, 500, where a, b, p, and q refer to NADH, oxalacetate, malate, and NAD+, respectively. The maximum velocity of the enzyme in human liver homogenates was 102 mumol/min/g wet wt of liver for oxalacetate reduction and 11.2 mumol/min/g liver for malate oxidation at pH 7.4 and 37 degrees C. Calculations using these parameters showed that, under conditions in vivo, the rate of NADH oxidation by the enzyme would be much less than the maximum velocity and could be comparable to the rate of NADH production during ethanol oxidation in human liver. The rate of NADH oxidation would be sensitive to the concentrations of NADH and oxalacetate; this sensitivity can explain the change in cytosolic NAD+/NADH redox state during ethanol metabolism in human liver.

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