Methylglyoxal as substrate and inhibitor of human aldehyde dehydrogenase: comparison of kinetic properties among the three isozymes.

@article{Izaguirre1998MethylglyoxalAS,
  title={Methylglyoxal as substrate and inhibitor of human aldehyde dehydrogenase: comparison of kinetic properties among the three isozymes.},
  author={Gonzalo Izaguirre and A Kikonyogo and Regina Pietruszko},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={1998},
  volume={119 4},
  pages={747-54}
}
Methylglyoxal was demonstrated to be a substrate for the isozymes E1, E2 and E3 of human aldehyde dehydrogenase. Pyruvate was the product from the oxidation of methylglyoxal by the three isozymes. At pH 7.4 and 25 degrees C, the major and minor components of the E3 isozyme catalyzed the reaction with Vmax of 1.1 and 0.8 mumol NADH min-1 mg-1 protein, respectively, compared to 0.067 and 0.060 mumol NADH min-1 mg-1 protein for the E1 and E2 isozymes, respectively. The E2 isozyme had a K(m) for… CONTINUE READING

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