Michaelis-Menten Kinetics for Determining Enzymatic Activity of Lysostaphin

被引：0
|
作者：
V. I. Surovtsev
T. V. Fedorov
M. A. Borozdina
机构：
[1] Ministry of Public Health of Russian Federation,State Research Center of Applied Microbiology
[2] Ministry of Public Health of Russian Federation,State Research Center of Applied Microbiology
来源：
Biochemistry (Moscow) | 2004年 / 69卷
关键词：
lysostaphin; lysis; immobilized substrate; Michaelis-Menten equation;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The rate of lysostaphin-catalyzed lysis of staphylococci follows the Michaelis-Menten equation at [E]0 ≪ [S]0, i.e., the activity of the enzyme is proportional to its concentration. This equation is proposed for determining the specific activity of lysostaphin. The apparent activation energy of hydrolysis of pentaglycine bridges in Staphylococcus peptidoglycan is 77.9 kJ/mol.
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页码：754 / 756
页数：2
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