Corynebacterium glutamicum의 NADPH-specific glutamate dehydrogenase를 이용하여 NADPH, NH$_4$Cl, $alpha$-ketoglutarate의 기질에 대한 kinetics를 고찰하였다. 이들의 kinetic constants를 측정함으로서 정반응에로의 효소반응 기작은 첫번째 효소와 반응하는 기질이 NADPH 임을 확인할 수 있었다. Glutamate dehydrogenase 활성의 조절을 위한 metabolites의 효과를 고찰하여 본 결과 malate와 citrate 만이 효소에 억제 효과를 나타내었으며, potassium chloride는 효소활성에 가장 많은 영향을 주었다.
A 150-fold purified preparation of NADPH-specific glutamate dehydrogenase of Corynebacterium glutamicum (1) was used for the determination of kinetic parameters of the substrates, NADPH, NH$_4$Cl, and $alpha$-ketoglutarate in the direction of glutamate synthesis. The kinetic constants determined from this study suggest a biosynthetic role for the enzyme, Based on the analysis of the result derived from initial velocity, the reaction mechanism was postulated to be ordered addition with NADPH as a first substrate to bind in the forward direction. Of the several metabolites tested for a possible function in the regulation of glutamate dehydrogenase activity, only malate and citrate were appeared to have an appreciable influence on the enzyme, Potassium chloride showed to be the most effective for the enzyme activity.
