人肝脏精氨琥珀酸酶中的负协同性。

Negative cooperativity in human liver argininosuccinase.

作者信息

Carvajal N, Fernández M, Rodríguez J P, Martínez J

出版信息

Biochim Biophys Acta. 1982 Mar 4;701(3):408-9. doi: 10.1016/0167-4838(82)90245-x.

Abstract

The kinetic properties of argininosuccinase (L-argininosuccinate arginine-lyase, EC 4.3.2.1.) were investigated. Negative cooperativity was observed in the response of the enzyme to the substrate argininosuccinate and GTP behaved as a positive allosteric effector. These effects were observed in 60 mM potassium phosphate but not in 50 mM Tris-HCl. Structural changes in the protein molecule are suggested to explain previous observations of Michaelis-Menten kinetics for this enzyme.

摘要

对精氨琥珀酸酶（L-精氨琥珀酸精氨酸裂解酶，EC 4.3.2.1.）的动力学特性进行了研究。观察到该酶对底物精氨琥珀酸的反应存在负协同性，并且鸟苷三磷酸（GTP）表现为正别构效应剂。这些效应在60 mM磷酸钾中观察到，但在50 mM Tris-HCl中未观察到。有人提出蛋白质分子的结构变化可以解释此前观察到的该酶的米氏动力学现象。