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...

Description complète

Enregistré dans:
Détails bibliographiques
Auteurs principaux: Bradford, Harlan N., Micucci, Joseph A., Krishnaswamy, Sriram
Format: Artigo
Langue:Inglês
Publié: American Society for Biochemistry and Molecular Biology 2010
Sujets:
Enzyme Catalysis and Regulation
Accès en ligne: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
Tags: Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!

Documents similaires