Residue Asp-189 Controls both Substrate Binding and the Monovalent Cation Specificity of Thrombin

Journal of Biological Chemistry

Volumn 279, Issue 11, 2004, Pages 10103-10108

  Prasad, Swati ^a   Cantwell, Angelene M ^a   Bush, Leslie A ^a   Shih, Peter ^a   Xu, Hong ^a   Di Cera, Enrico ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD; COAGULATION; ENZYMES; MUTAGENESIS; POSITIVE IONS; SODIUM;

BLOOD COAGULATION; MONOVALENT CATIONS;

BIOCHEMISTRY;

ASPARAGINE; ASPARTIC ACID; GLUTAMIC ACID; MONOVALENT CATION; SERINE; THROMBIN; TRYPSIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CATALYSIS; CATION TRANSPORT; COMPLEMENT SYSTEM; CYTOARCHITECTURE; ENZYME BINDING; ENZYME SPECIFICITY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RESIDUE ANALYSIS; SITE DIRECTED MUTAGENESIS; TISSUE SPECIFICITY;

ALANINE; ALLOSTERIC SITE; ASPARAGINE; ASPARTIC ACID; BINDING SITES; CATIONS; DOSE-RESPONSE RELATIONSHIP, DRUG; GLUTAMINE; HUMANS; HYDROLYSIS; IONS; KINETICS; LITHIUM; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; RUBIDIUM; SERINE; SODIUM; SUBSTRATE SPECIFICITY; THROMBIN; TRYPSIN;

ANIMALIA;

EID: 1642269650     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M312614200     Document Type: Article

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