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...

Πλήρης περιγραφή

Αποθηκεύτηκε σε:
Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς: Bradford, Harlan N., Micucci, Joseph A., Krishnaswamy, Sriram
Μορφή: Artigo
Γλώσσα:Inglês
Έκδοση: American Society for Biochemistry and Molecular Biology 2010
Θέματα:
Enzyme Catalysis and Regulation
Διαθέσιμο Online: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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