Effect of cryosolvent on transient kinetics of the glutamate dehydrogenase reaction.
Effect of cryosolvent on transient kinetics of the glutamate dehydrogenase reaction.
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DOI：
10.1021/bi00269a012
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发表时间：
1982-12
期刊：
影响因子：
2.9
通讯作者：
A. Colen;R. E. Johnson;H. F. Fisher
中科院分区：
文献类型：
--
作者：
A. Colen;R. E. Johnson;H. F. Fisher
The transient and steady-state kinetics of the oxidative deamination of L-glutamate by glutamate dehydrogenase and NADP in both aqueous solution and 30% methanol are compared. Methanol causes an approximately 5-fold tightening of the enzyme--L-glutamate binary complex and an approximately 2-fold reduction of the interaction parameter for the ternary enzyme--NADP--L-glutamate complex. The most dramatic effect of methanol on the time course of the reaction is what appears to be a conversion of the enzyme at substoichiometric initial levels of reactant NADP to a form from which product alpha-ketoglutarate does not readily dissociate. This conversion appears only at NADP concentrations over one-third of the enzyme active site concentration.
