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

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  • KAWAKAMI Ryushi
    Analytical Research Center for Experimental Sciences, Saga University
  • OYAMA Masaki
    Department of Applied Biochemistry and Food Science, Faculty of Agriculture, Saga University
  • SAKURABA Haruhiko
    Department of Applied Biological Science, Faculty of Agriculture, Kagawa University
  • OHSHIMA Toshihisa
    Microbial Genetics Division, Institute of Genetic Resources, Faculty of Agriculture, Kyushu University

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  • The Unique Kinetic Behavior of the Very Large NAD-Dependent Glutamate Dehydrogenase from<i>Janthinobacterium lividum</i>

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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 10 mM L-aspartate.

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