Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase.

doi:10.1021/bi00244a014

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Article

Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase.

Biochemistry - 30 Jul 1991

Toney M D, Kirsch J F

Abstract excerpt

The Y70F mutant of aspartate aminotransferase has reduced affinity for coenzymes compared to the wild type. The equilibrium dissociation constants for pyridoxamine phosphate (PMP) holoenzymes, KPMPdiss, were determined from the association and dissociation rate constants to be 1.3 nM and 30 nM fo...

Topics

Apoenzymes
Aspartate Aminotransferases
Coenzymes
Escherichia coli
Glutamates
Glutamic Acid
Hydrogen Bonding
Ketoglutaric Acids
Kinetics
Mutation
Pyridoxal Phosphate
Pyridoxamine

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