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个人信息Personal Information
教授
博士生导师
硕士生导师
主要任职：Director, State Key laboratory of Fine Chemicals
其他任职：精细化工国家重点实验室主任、国务院学科评议组成员
性别：男
毕业院校：大连理工大学
学位：博士
所在单位：化工学院
学科：应用化学. 精细化工. 化学生物学
办公地点：大连理工大学精细化工国家重点实验室
西部校区化工实验楼F-202#
http://peng-group.dlut.edu.cn/
联系方式：大连理工大学精细化工国家重点实验室 西部校区化工实验楼F-202 辽宁省大连市高新区凌工路2号，大连116024 Tel: 0411-84986306; Fax: 0411-84986292；课题组网址：http://peng-group.dlut.edu.cn/
电子邮箱：pengxj@dlut.edu.cn
Kinetics of inactivation of Ulva pertusa Kjellm alkaline phosphatase by ethylenediaminetetraacetic acid disodium
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论文类型：期刊论文
发表时间：2001-10-01
发表刊物：JOURNAL OF ENZYME INHIBITION
收录刊物：Scopus、SCIE、PubMed
卷号：16
期号：4
页面范围：313-319
ISSN号：8755-5093
关键字：alkaline phosphatase; kinetics; inactivation; zinc ion
摘要：Ova pertusa Kjellm alkaline phosphatase (EC 3.3.3.1) is a metalloenzyme, the active site of which contains a tight cluster of two zinc ions and one magnesium ion. The kinetic theory described by Tsou of the substrate reaction during irreversible inhibition of enzyme activity has been employed to study the kinetics of the course of inactivation of the enzyme by EDTA. The kinetics of the substrate reaction at different concentrations of the substrate p-nitrophenyl phosphate (PNPP) and inactivator EDTA indicated a complexing mechanism for inactivation by, and substrate competition with, EDTA at the active site. The inactivation kinetics are single phasic, showing that the initial formation of an enzyme EDTA complex is a relative rapid reaction, following by a slow inactivation step that probably involves a conformational change of the enzyme. The presence of Zn2+ apparently stabilizes an active-site conformation required for enzyme activity.