Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 29, 2005, Pages 10099-10104

  Bianchini, Elsa P ^a   Orcutt, Steven J ^a   Panizzi, Peter ^c   Bock, Paul E ^c   Krishnaswamy, Sriram ^a,b  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c VANDERBILT UNIVERSITY   (United States)

Author keywords

Blood coagulation; Enzymology; Proteolytic cleavage; Serine protease; Zymogen activation

Indexed keywords

ARGININE; BLOOD CLOTTING FACTOR 10A; ENZYME INHIBITOR; ENZYME PRECURSOR; MEIZOTHROMBIN; MUTANT PROTEIN; PROTEINASE; PROTHROMBIN; THROMBIN;

ARTICLE; CATALYST; CHEMICAL BOND; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISSOCIATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN SYNTHESIS; THERMODYNAMICS;

BINDING SITES; ENZYME ACTIVATION; ENZYME PRECURSORS; FLUORESCENCE; HUMANS; KINETICS; MODELS, MOLECULAR; MUTATION; NITRACRINE; PROTEIN CONFORMATION; PROTHROMBIN; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THROMBIN; THROMBOPLASTIN;

EID: 22544469092     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0504704102     Document Type: Article

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