Thrombin: a paradigm for enzymes allosterically activated by monovalent cations

被引：29

作者：

Di Cera, E ^{[1
]}

机构：

[1] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA

来源：

COMPTES RENDUS BIOLOGIES | 2004年 / 327卷 / 12期

关键词：

thrombin; monovalent cations; monovalent-cation-activated enzymes; allostery; serine proteases; evolution;

D O I：

10.1016/j.crvi.2004.07.011

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Enzymes activated by monovalent cations are abundantly represented in plants and in the animal world. The mechanism of activation involves formation of a ternary intermediate with the enzyme-substrate complex, or binding of the cation to an allosteric site in the protein. Thrombin is a Na+-activated enzyme with procoagulant, anticoagulant and signaling roles. The binding of Na+ influences allosterically thrombin function and offers a paradigm for regulatory control of protease activity and specificity. Here we review the molecular basis of thrombin allostery as recently emerged from mutagenesis and structural studies. The role of Na+ in blood coagulation and the evolution of serine proteases are also discussed. (C) 2004 Academie des sciences. Published by Elsevier SAS. All rights reserved.

引用

页码：1065 / 1076

页数：12

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