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Kinetic properties of glutaminase from pig renal cortex.

Kinetic properties of two enzyme forms of purified pig kidney glutaminase, the phosphateborate and Tris-Cl enzymes, have been investigated. Plots of velocity versus phosphate concentration are sigmoidal for both forms. However, with α-ketoglutarate present, double reciprocal plots of velocity versus phosphate are linear for the phosphate-borate enzyme, and parabolic for the Tris-Cl enzyme. Inhibition by glutamate is non-competitive for the phosphate-borate enzyme, and competitive for the Tris-Cl enzyme. Moreover, with α-ketoglutarate present, phosphate activates the phosphate-borate enzyme only slightly, but it counteracts the inhibitory effect of glutamate strongly. When glutamine is the variable substrate, phosphate decreases the apparent Michaelis constant and increases maximal velocity for both enzyme forms. 
 
 
 
Using glutamate as the fixed variable and glutamine as the variable substrate, double reciprocal plots are linear, showing non-competitive inhibition between glutamine and glutamate for both enzyme forms. Replots of slopes versus glutamate are non-linear and of intercepts versus glutamate, linear. The experimental data are explained by assuming an ordered mechanism in which glutamate is the first product to be released.