Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): The importance of acidic residues in the double e loop

Journal of Biological Chemistry

Volumn 289, Issue 47, 2014, Pages 32604-32616

  Feng, You ^a   Hadjikyriacou, Andrea ^a   Clarke, Steven G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; ARGININE; ENZYME ACTIVITY; NUCLEIC ACIDS; PROTEINS; TEMPERATURE DISTRIBUTION;

BIOLOGICAL FUNCTIONS; C-TERMINAL DOMAINS; CELL DIFFERENTIATION; ENZYMATIC MECHANISMS; PROTEIN-ARGININE METHYLTRANSFERASE; SITE DIRECTED MUTAGENESIS; SUBSTRATE SPECIFICITY; TEMPERATURE DEPENDENCE;

SUBSTRATES;

ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; HYBRID PROTEIN; N(G) METHYLARGININE; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 7; UNCLASSIFIED DRUG; CATION; GLUTATHIONE TRANSFERASE; HISTONE; PRMT7 PROTEIN, HUMAN;

ACIDITY; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; METHYLATION; PROTEIN EXPRESSION; PROTEIN MOTIF; SALT TOLERANCE; SITE DIRECTED MUTAGENESIS; TEMPERATURE DEPENDENCE; AMINO ACID SEQUENCE; BIOCATALYSIS; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; HUMAN; ION EXCHANGE CHROMATOGRAPHY; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROCEDURES; SEQUENCE HOMOLOGY; TEMPERATURE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ASPARTIC ACID; BIOCATALYSIS; CATALYTIC DOMAIN; CATIONS; CHROMATOGRAPHY, ION EXCHANGE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUTAMIC ACID; GLUTATHIONE TRANSFERASE; HISTONES; HUMANS; KINETICS; METHYLATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN-ARGININE N-METHYLTRANSFERASES; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84911908602     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.609271     Document Type: Article

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