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The unique kinetic behavior of the very large NAD-dependent glutamate dehydrogenase from Janthinobacterium lividum
Ryushi Kawakami1, Masaki Oyama, Haruhiko Sakuraba
1Analytical Research Center for Experimental Sciences, Saga University, Japan.
Abstract:
The kinetics of a very large NAD-dependent glutamate dehydrogenase from Janthinobacterium lividum showed positive cooperativity toward alpha-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 alpha-ketoglutarate and NADH with the addition of L-aspartate, and the kinetic response for alpha-ketoglutarate changed completely to a typical Michaelis-Menten type in the presence of 10 mM L-aspartate.
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