Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin

Journal of Biological Chemistry

Volumn 279, Issue 52, 2004, Pages 54927-54936

  Orcutt, Steven J ^a   Krishnaswamy, Sriram ^a,b  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; BINDING ENERGY; CATALYSIS; DATA REDUCTION; ENZYMES;

BINDING INTERACTIONS; CLEAVAGE REACTIONS; PROTHROMBINASE;

MOLECULAR STRUCTURE;

ARGININE; BLOOD CLOTTING FACTOR 10A; PROTHROMBIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; COMPETITIVE INHIBITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN INTERACTION; REACTION ANALYSIS; REDUCTION; STRUCTURE ACTIVITY RELATION; THROMBOGENESIS; WILD TYPE;

AMINO ACID SEQUENCE; ARGININE; BINDING SITES; CELL LINE; CLONING, MOLECULAR; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; KINETICS; MUTAGENESIS, INSERTIONAL; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTHROMBIN; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THROMBOPLASTIN; TRANSFECTION;

EID: 11144229671     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M410866200     Document Type: Article

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