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Volumn 41, Issue 2, 2002, Pages 537-546
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Two glutamate residues, Glu 208α and Glu 197β, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase
a
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Author keywords
[No Author keywords available]
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Indexed keywords
MUTANTS;
CATALYSIS;
CONFORMATIONS;
CRYSTAL STRUCTURE;
ENZYMES;
ESCHERICHIA COLI;
PROTEINS;
BIOCHEMISTRY;
GLUTAMATE RECEPTOR;
GLUTAMINE;
HISTIDINE;
SUCCINYL COENZYME A SYNTHETASE;
ALPHA CHAIN;
ANIMAL CELL;
ARTICLE;
CATALYSIS;
DEPHOSPHORYLATION;
ENZYME ACTIVE SITE;
ENZYME PHOSPHORYLATION;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
REACTION ANALYSIS;
RESIDUE ANALYSIS;
SITE DIRECTED MUTAGENESIS;
STRUCTURE ANALYSIS;
ADENOSINE;
ALANINE;
ASPARTIC ACID;
BINDING SITES;
CATALYSIS;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ESCHERICHIA COLI;
GLUTAMIC ACID;
HISTIDINE;
HYDROGEN BONDING;
KINETICS;
MODELS, CHEMICAL;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PHOSPHORYLATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
SUCCINATE-COA LIGASES;
TIME FACTORS;
ANIMALIA;
ESCHERICHIA COLI;
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EID: 0037080163
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011518y Document Type: Article |
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Times cited : (25)
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References (40)
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