The unique kinetic behavior of the very large NAD-dependent glutamate dehydrogenase from janthinobacterium lividum

Abstract

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 S0:5 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 10mM L-aspartate.