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Volumn 281, Issue 15, 2006, Pages 9925-9934
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Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase
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Author keywords
[No Author keywords available]
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Indexed keywords
CELLS;
ENZYMES;
ESCHERICHIA COLI;
METALLOIDS;
MOLECULAR BIOLOGY;
MUTAGENESIS;
ARSRDABC OPERON;
ESCHERICHIA COLI PLASMID R773;
SIGNAL TRANSDUCTION;
BIOCHEMISTRY;
ADENOSINE TRIPHOSPHATASE;
ANTIMONY;
ARSAB ENZYME;
ARSENIC TRIOXIDE;
CYSTEINE;
MAGNESIUM;
NUCLEOTIDE;
PROTEIN ARSA;
PROTEIN ARSB;
PROTEIN SUBUNIT;
UNCLASSIFIED DRUG;
ADENOSINE TRIPHOSPHATE;
ANTIMONY TARTRATE;
ARSAB ATPASE, E COLI;
ARSENITE SODIUM;
ARSENOUS ACID DERIVATIVE;
ESCHERICHIA COLI PROTEIN;
MULTIENZYME COMPLEX;
OLIGONUCLEOTIDE;
SODIUM DERIVATIVE;
TRYPSIN;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
CODON;
CONTROLLED STUDY;
ENZYME ACTIVITY;
ENZYME BINDING;
ENZYME SUBUNIT;
ESCHERICHIA COLI;
GENE EXPRESSION;
INDUCED MUTATION;
ION TRANSPORT;
METAL BINDING;
MOLECULAR EVOLUTION;
NONHUMAN;
NUCLEOTIDE BINDING SITE;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN PURIFICATION;
TRANSPORT KINETICS;
WILD TYPE;
CATALYSIS;
CHEMICAL MODEL;
CHEMICAL STRUCTURE;
CHEMISTRY;
DOSE RESPONSE;
ENZYME ACTIVE SITE;
HYDROLYSIS;
METABOLISM;
MUTATION;
PHYSIOLOGY;
PLASMID;
PROTEIN BINDING;
PROTEIN CONFORMATION;
SITE DIRECTED MUTAGENESIS;
TIME;
ESCHERICHIA COLI;
ADENOSINE TRIPHOSPHATASES;
ADENOSINE TRIPHOSPHATE;
ANTIMONY POTASSIUM TARTRATE;
ARSENITES;
BINDING SITES;
CATALYSIS;
CATALYTIC DOMAIN;
CODON;
CYSTEINE;
DOSE-RESPONSE RELATIONSHIP, DRUG;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
HYDROLYSIS;
ION PUMPS;
MAGNESIUM;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MULTIENZYME COMPLEXES;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
NUCLEOTIDES;
OLIGONUCLEOTIDES;
PLASMIDS;
PROTEIN BINDING;
PROTEIN CONFORMATION;
SODIUM COMPOUNDS;
TIME FACTORS;
TRYPSIN;
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EID: 33744508953
PISSN: 00219258
EISSN: 1083351X
Source Type: Journal
DOI: 10.1074/jbc.M600125200 Document Type: Article |
Times cited : (30)
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References (23)
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