The Unique Kinetic Behavior of the Very Large NAD-Dependent Glutamate Dehydrogenase fromJanthinobacterium lividum
Author(s) -
Ryushi Kawakami,
Masaki Oyama,
Haruhiko Sakuraba,
Toshihisa Ohshima
Publication year - 2010
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.90925
Subject(s) - nad+ kinase , glutamate dehydrogenase , kinetic energy , chemistry , biology , physics , glutamate receptor , biochemistry , enzyme , classical mechanics , receptor
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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