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Volumn 10, Issue 12, 1997, Pages 1415-1424
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A glutamine 67→histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition
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Author keywords
Folate; Isothermal titration calorimetry; NADPH; R plasmid; Site directed mutagenesis
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Indexed keywords
BACTERIAL ENZYME;
DIHYDROFOLATE REDUCTASE;
FOLIC ACID;
GLUTAMINE;
HISTIDINE;
MUTANT PROTEIN;
REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
TETRAMER;
DIHYDROFOLIC ACID;
DRUG DERIVATIVE;
ENZYME INHIBITOR;
HISTAMINE;
NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;
AMINO ACID SUBSTITUTION;
ARTICLE;
BINDING KINETICS;
BINDING SITE;
CALORIMETRY;
CATALYSIS;
CONTROLLED STUDY;
ENZYME ACTIVE SITE;
ENZYME BINDING;
ENZYME INHIBITION;
ENZYME SUBSTRATE COMPLEX;
LIGAND BINDING;
PRIORITY JOURNAL;
STRUCTURE ACTIVITY RELATION;
CHEMISTRY;
ESCHERICHIA COLI;
GENETICS;
KINETICS;
MACROMOLECULE;
METABOLISM;
SITE DIRECTED MUTAGENESIS;
THERMODYNAMICS;
BINDING SITES;
CALORIMETRY;
CATALYSIS;
ENZYME INHIBITORS;
ESCHERICHIA COLI;
FOLIC ACID;
GLUTAMINE;
HISTAMINE;
KINETICS;
MACROMOLECULAR SUBSTANCES;
MUTAGENESIS, SITE-DIRECTED;
NADP;
STRUCTURE-ACTIVITY RELATIONSHIP;
TETRAHYDROFOLATE DEHYDROGENASE;
THERMODYNAMICS;
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EID: 0031282924
PISSN: 02692139
EISSN: None
Source Type: Journal
DOI: 10.1093/protein/10.12.1415 Document Type: Article |
Times cited : (30)
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References (30)
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