The Unique Kinetic Behavior of the Very Large NAD-Dependent Glutamate Dehydrogenase from Janthinobacterium lividum

抄録

The kinetics of a very large NAD-dependent glutamate dehydrogenase from Janthinobacterium lividum showed positive cooperativity toward α-ketoglutarate and NADH, and the Michaelis-Menten type toward ammonium chloride in the absence of the catalytic activator, L-aspartate. An increase in the maximum activity accompanied the decrease in the S_0.5 values for α-ketoglutarate and NADH with the addition of L-aspartate, and the kinetic response for α-ketoglutarate changed completely to a typical Michaelis-Menten type in the presence of 10 mM L-aspartate.