Hudson R C, Daniel R M
Microbial Biochemistry and Biotechnology Unit, School of Science and Technology, University of Waikato, Hamilton, New Zealand.
Biochim Biophys Acta. 1995 Jul 3;1250(1):60-8. doi: 10.1016/0167-4838(95)00043-t.
A steady state kinetic study was carried out with the glutamate dehydrogenase from the thermophilic, archaebacterial isolate AN1. Initial velocity studies of the oxidative deamination reaction showed the mechanism is sequential and indicated that the order of substrate addition is random, while inhibition studies with products and substrate analogues suggested a strong preference for NADP+ to bind first. Initial velocity studies of the reductive amination reaction showed that the mechanism is sequential and indicated that the order of substrate addition is random, while product inhibition studies and the effect of substrate saturation on the initial velocity suggested that the preferred order of substrate addition is NADPH, 2-ketoglutarate, ammonia.
对嗜热古细菌分离株AN1的谷氨酸脱氢酶进行了稳态动力学研究。氧化脱氨反应的初始速度研究表明，其机制是有序的，底物添加顺序是随机的，而产物和底物类似物的抑制研究表明，强烈倾向于NADP+先结合。还原胺化反应的初始速度研究表明，其机制是有序的，底物添加顺序是随机的，而产物抑制研究以及底物饱和度对初始速度的影响表明，底物添加的优先顺序是NADPH、2-酮戊二酸、氨。
