Abstract
1. 1. The glutamate dehydrogenase of mussel hepatopancreas is NAD(H) dependent and shows absolute requirement for ADP as cofactor. 2. 2. The optimum pH for GDH lies between 7.4 and 8.2 (reductive amination) and 9.5 (oxidative deamination). The enzyme has an activation energy of 53.9 kJ/mol and an average Q 10 of 1.65. 3. 3. ADP and 2-oxoglutarate stabilize the enzyme, while NADH diminishes the stabilization significantly. 4. 4. In the sense of reductive amination the apparent K m values are 0.38 mM for 2-oxoglutarate, 34 μM for NADH and 20 mM for NH 4 +. In the opposite sense the apparent K m for glutamate is 5 mM and 0.55 mM for NAD +.
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