STEADY-STATE KINETICS OF ENZYMES WITH SUBSTRATES HAVING MULTIPLE REACTION SITES

被引：1

作者：

BARNSLEY, EA

机构：

[1] Department of Biochemistry, Memorial University, St. John's

来源：

JOURNAL OF THEORETICAL BIOLOGY | 1990年 / 142卷 / 02期

关键词：

D O I：

10.1016/S0022-5193(05)80228-0

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An enzyme catalysing the reaction of a substrate with multiple reaction sites may display steady state kinetics described by a Michaels-Menten equation. The Km is identical for all sites considered individually and all sites together. The maximum velocity for a single site depends on the rate constants for reaction at that site and at all of other sites. © 1990 Academic Press Limited.

引用

页码：275 / 279

页数：5

共 3 条

[1] ISOLATION AND CHARACTERIZATION OF SHEEP PEPSIN [J].