Plaut B, Knowles J R
Biochem J. 1972 Sep;129(2):311-20. doi: 10.1042/bj1290311.
The pH-dependences of the kinetic parameters k(cat.) and K(m) for the triose phosphate isomerase reaction were determined in each direction. Apparent pK(a) values of 6.0 and 9.0 are observed in the dependences of k(cat.)/K(m). The pH-dependences of k(cat.) are sigmoid, with apparent pK(a) values of about 6.0. The results are interpreted in terms of a single base on the enzyme providing an efficient proton-shuttling mechanism for the isomerization.
在两个方向上测定了磷酸丙糖异构酶反应动力学参数k(cat.)和K(m)的pH依赖性。在k(cat.)/K(m)的依赖性中观察到表观pK(a)值为6.0和9.0。k(cat.)的pH依赖性呈S形,表观pK(a)值约为6.0。结果表明,酶上的单个碱基为异构化提供了一种有效的质子穿梭机制。