Substrate specificity, processivity, and kinetic mechanism of protein arginine methyltransferase 5

Biochemistry

Volumn 52, Issue 32, 2013, Pages 5430-5440

  Wang, Min ^a   Xu, Rui Ming ^b   Thompson, Paul R ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b INSTITUTE OF BIOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS ELEGANS; DEAD-END INHIBITIONS; DIMETHYLATED ARGININES; DNA DAMAGING AGENTS; METHYLTRANSFERASES; PROTEIN-ARGININE METHYLTRANSFERASE; SUBSTRATE SPECIFICITY; THERAPEUTIC TARGETS;

DISEASES; ENZYMES; PROTEINS;

ARGININE;

PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 5; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; HYDROGEN BOND; MICHAELIS CONSTANT; PRIORITY JOURNAL; PROTEIN METHYLATION; STEADY STATE;

AMINO ACID SEQUENCE; ANIMALS; ARGININE; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CATALYSIS; KINETICS; METHYLATION; MOLECULAR SEQUENCE DATA; PROTEIN-ARGININE N-METHYLTRANSFERASES; SUBSTRATE SPECIFICITY;

EID: 84881648776     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4005123     Document Type: Article

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