Thrombin: a paradigm for enzymes allosterically activated by monovalent cations

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Abstract
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. To cite this article: E. Di Cera, C. R. Biologies 327 (2004).