Residues in Human Arsenic (+3 Oxidation State) Methyltransferase Forming Potential Hydrogen Bond Network around S-adenosylmethionine

PLoS ONE

Volumn 8, Issue 10, 2013, Pages

  Li, Xiangli ^a   Cao, Jing ^a   Wang, Shuping ^a   Geng, Zhirong ^a   Song, Xiaoli ^b   Hu, Xin ^c   Wang, Zhilin ^a  

^a NANJING UNIVERSITY   (China)

^b YANGZHOU UNIVERSITY   (China)

^c NANJING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; AMINO ACID DERIVATIVE; ARSENIC; ARSENIC DERIVATIVE; ARSENIC METHYLTRANSFERASE; GLUTAMIC ACID; GLUTAMINE; GLYCINE; HYDROGEN; INORGANIC COMPOUND; ISOLEUCINE; METHIONINE; METHYLTRANSFERASE; MONOMETHYLATED ARSENICAL; MUTANT PROTEIN; S ADENOSYLMETHIONINE; SERINE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL BINDING; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME CONFORMATION; HYDROGEN BOND; MICHAELIS CONSTANT; OXIDATION; RESIDUE ANALYSIS;

AMINO ACIDS; ARSENIC; BINDING SITES; CATALYSIS; GENE EXPRESSION; HUMANS; HYDROGEN BONDING; KINETICS; METHYLATION; METHYLTRANSFERASES; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; S-ADENOSYLMETHIONINE; SUBSTRATE SPECIFICITY;

EID: 84885037515     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0076709     Document Type: Article

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