Glutamate Carboxypeptidase II - Enzyme Kinetics

Enzyme Kinetics

The hydrolysis of NAAG by GCPII obeys Michaelis-Menten kinetics calculated the binding constant (Km) for NAAG as approximately 130 nM and the turnover constant (kcat) as approximately 4 s−1. The apparent second-order rate constant is approximately 3 x 107 (M·s)−1.

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