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Volumn 91, Issue 9, 2009, Pages 801-809
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Deciphering interactions of the aminoglycoside phosphotransferase(3′)-IIIa with its ligands
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Author keywords
Aminoglycosides; Antibiotic resistance; Enzyme ligand interactions; Phosphoryl transfer reaction; Thermodynamics
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Indexed keywords
AMINOGLYCOSIDE ANTIBIOTICS;
AMINOGLYCOSIDES;
ANTIBIOTIC RESISTANCE;
APO-ENZYMES;
BINDING AFFINITIES;
CATALYTIC RATES;
DISSOCIATION CONSTANT;
DIVALENT CATION;
ELECTRON PARAMAGNETIC RESONANCE;
ENZYME-LIGAND INTERACTIONS;
ENZYME-SUBSTRATE COMPLEXES;
HIGH AFFINITY;
METAL BINDING;
METAL BINDING SITES;
PHOSPHORYL TRANSFER REACTION;
PHOSPHOTRANSFERASES;
SUBSTRATE RANGE;
SUBSTRATE SELECTIVITY;
THERMODYNAMIC CHARACTERIZATION;
PHOSPHORYL TRANSFER;
ANTIBIOTICS;
BINDING ENERGY;
BINDING SITES;
DISSOCIATION;
ENZYMES;
FLUORESCENCE SPECTROSCOPY;
LIGANDS;
MAGNESIUM;
MANGANESE;
NUCLEOTIDES;
PARAMAGNETIC RESONANCE;
PARAMAGNETISM;
POSITIVE IONS;
SULFUR COMPOUNDS;
THERMODYNAMICS;
SUBSTRATES;
ADENOSINE TRIPHOSPHATE;
AMIKACIN;
AMINOGLYCOSIDE ANTIBIOTIC AGENT;
AMINOGLYCOSIDE PHOSPHOTRANSFERASE IIIA;
APOENZYME;
BUTIROSIN;
DIVALENT CATION;
KANAMYCIN A;
MAGNESIUM;
MANGANESE;
NEOMYCIN;
PHOSPHOTRANSFERASE;
SISOMICIN;
UNCLASSIFIED DRUG;
AMINOGLYCOSIDE;
ISOENZYME;
KANAMYCIN KINASE;
LIGAND;
METAL;
NUCLEOTIDE;
AMINOGLYCOSIDE DERIVATIVE;
AMINOGLYCOSIDE PHOSPHOTRANSFERASE(3') IIIA;
ARTICLE;
BINDING AFFINITY;
BINDING SITE;
DISSOCIATION CONSTANT;
DRUG PROTEIN BINDING;
ELECTRON SPIN RESONANCE;
ENZYME BINDING;
ENZYME SUBSTRATE COMPLEX;
FLUORESCENCE SPECTROSCOPY;
METAL BINDING;
THERMODYNAMICS;
CHEMICAL STRUCTURE;
CHEMISTRY;
METABOLISM;
PROTEIN BINDING;
PROTEIN CONFORMATION;
ANTIBIOTIC RESISTANCE;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME SPECIFICITY;
LIGAND BINDING;
NUCLEOTIDE BINDING SITE;
PROTEIN PROTEIN INTERACTION;
STOICHIOMETRY;
AMINOGLYCOSIDES;
ELECTRON SPIN RESONANCE SPECTROSCOPY;
ISOENZYMES;
KANAMYCIN KINASE;
LIGANDS;
METALS;
MODELS, MOLECULAR;
MOLECULAR STRUCTURE;
NUCLEOTIDES;
PROTEIN BINDING;
PROTEIN CONFORMATION;
THERMODYNAMICS;
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EID: 70149116332
PISSN: 00063525
EISSN: 10970282
Source Type: Journal
DOI: 10.1002/bip.21251 Document Type: Article |
Times cited : (12)
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References (28)
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