Kawakami Ryushi, Oyama Masaki, Sakuraba Haruhiko, Ohshima Toshihisa
Analytical Research Center for Experimental Sciences, Saga University, Japan.
Biosci Biotechnol Biochem. 2010;74(4):884-7. doi: 10.1271/bbb.90925. Epub 2010 Apr 7.
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.
来自青紫色杆菌的一种非常大的NAD依赖型谷氨酸脱氢酶的动力学表明，在没有催化激活剂L-天冬氨酸的情况下，对α-酮戊二酸和NADH表现出正协同性，对氯化铵表现出米氏类型。添加L-天冬氨酸后，最大活性增加，同时α-酮戊二酸和NADH的S(0.5)值降低，在存在10 mM L-天冬氨酸的情况下，α-酮戊二酸的动力学响应完全转变为典型的米氏类型。
