Kinetic mechanism of argininosuccinate synthetase.
Kinetic mechanism of argininosuccinate synthetase.
复制标题
精氨基琥珀酸合成酶的动力学机制。
DOI：
10.1016/0003-9861(83)90114-5
复制
发表时间：
1983
影响因子：
3.9
通讯作者：
Seiglie,JL
中科院分区：
文献类型：
--
作者：
Raushel,FM;Seiglie,JL
测定了pH为7.5时牛肝精氨酸琥珀酸合成酶的动力学机制。初始速度、产物和终端抑制模式与MgATP、瓜氨酸和天冬氨酸的有序加入、精氨酸琥珀酸、MgPPi和AMP的有序释放一致，其机制也与瓜氨酸腺苷酸作为反应中间体的形成一致[0]。Rochovansky和S. Ratner,（1967）。医学杂志。化学。, 242, 3839 - 3849]。在三种底物中的任何一种都没有得到非线性双倒易图的证据。
The kinetic mechanism of bovine liver argininosuccinate synthetase has been determined at pH 7.5. The initial velocity and product and dead-end inhibition patterns are consistent with the ordered addition of MgATP, citrulline, and aspartate, followed by the ordered release of argininosuccinate, MgPPi, and AMP. The mechanism is also in accord with the formation of citrulline-adenylate as a reactive intermediate [O. Rochovansky, and S. Ratner, (1967)J. Biol. Chem.,242, 3839–3849]. No evidence was obtained for nonlinear double-reciprocal plots with any of the three substrates.