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Rabbit muscle pyruvate kinase catalyzes the hydrolysis of P-enolpyruvate at the same active site which catalyzes the physiologically important kinase reaction. The hydrolase activity is lower than the kinase activity by a factor of at least 10(3). There are specific monovalent cation and divalent cation requirements. No other cofactors are required. The relative activation of the pyruvate kinase for the hydrolase reaction is: Ni(II) greater than Co(II) greater than Mg(II) greater than Mn(II). This parallels the rates of nonenzymatic hydrolysis of P-enolpyruvate (Benkovic, S.J., and Schray, K.J. (1968) Biochemistry 7, 4097-4102). The pH rate profiles of the hydrolase and kinase reactions activated by Ni(II) and Co(II) are similar, suggesting common features in their mechanisms. In contrast to the kinase reaction, the reaction velocity of the hydrolase increases at high Co(II) concentrations indicating a second mode for hydrolysis.
K Erhard, and
R C Davis
July 1971,
Biochemistry,
K Erhard, and
R C Davis
February 1972,
Biochemistry,
K Erhard, and
R C Davis
January 1972,
Biochemical and biophysical research communications,
K Erhard, and
R C Davis
March 1981,
European journal of biochemistry,
K Erhard, and
R C Davis
May 1981,
The Journal of biological chemistry,
K Erhard, and
R C Davis
March 1969,
The Journal of biological chemistry,
K Erhard, and
R C Davis
February 1981,
Biochemistry,
K Erhard, and
R C Davis
February 1973,
The Biochemical journal,
K Erhard, and
R C Davis
June 1988,
Archivos de biologia y medicina experimentales,
K Erhard, and
R C Davis
March 1983,
The Biochemical journal,
