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

Ryushi Kawakami, Masaki Oyama, Haruhiko Sakuraba, Toshihisa Ohshima

Journal: Bioscience, biotechnology, and biochemistry 2010;74(4):884-7

PMID: 20378971

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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.

Address: Analytical Research Center for Experimental Sciences, Saga University, Japan.

DOI: 10.1271/bbb.90925

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MeSH Terms: Aspartic Acid, Catalysis, Chromobacterium, Glutamate Dehydrogenase, Glutamic Acid, Ketoglutaric Acids, Kinetics, NAD, Oxalobacteraceae