The unique kinetic behavior of the very large NAD-dependent glutamate dehydrogenase from Janthinobacterium lividum.
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.
Kawakami
Ryushi
R
Analytical Research Center for Experimental Sciences, Saga University, Japan.
Oyama
Masaki
M
Sakuraba
Haruhiko
H
Ohshima
Toshihisa
T
D001224:Aspartic Acid; D002384:Catalysis; D002861:Chromobacterium / Q000378:metabolism; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D018698:Glutamic Acid; D007656:Ketoglutaric Acids; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D042802:Oxalobacteraceae / Q000378:metabolism
D007656:Ketoglutaric Acids; D009243:NAD; D001224:Aspartic Acid; D018698:Glutamic Acid; D005969:Glutamate Dehydrogenase