Regulated Cleavage of Prothrombin by Prothrombinase: REPOSITIONING A CLEAVAGE SITE REVEALS THE UNIQUE KINETIC BEHAVIOR OF THE ACTION OF PROTHROMBINASE ON ITS COMPOUND SUBSTRATE

Prothrombinase converts prothrombin to thrombin via cleavage at Arg(320) followed by cleavage at Arg(271). Exosite-dependent binding of prothrombin to prothrombinase facilitates active site docking by Arg(320) and initial cleavage at this site. Precise positioning of the Arg(320) site for cleavage i...

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Detalhes bibliográficos
Main Authors: Bradford, Harlan N., Micucci, Joseph A., Krishnaswamy, Sriram
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2010
Assuntos:
Enzyme Catalysis and Regulation
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2804180/
https://ncbi.nlm.nih.gov/pubmed/19858193
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.070334
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