Protein dynamics control the progression and efficiency of the catalytic reaction cycle of the Escherichia coli DNA-repair enzyme AlkB

Journal of Biological Chemistry

Volumn 289, Issue 43, 2014, Pages 29584-29601

  Ergel, Burҫe ^a   Gill, Michelle L ^a   Brown, Lewis ^a   Yu, Bomina ^a   Palmer, Arthur G ^a   Hunt, John F ^a  

^a Columbia University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CONFORMATIONS; DYNAMICS; EFFICIENCY; ESCHERICHIA COLI; REACTION INTERMEDIATES; REPAIR;

BIOPHYSICAL STUDIES; CATALYTIC REACTIONS; COMPLEX CHEMICAL REACTIONS; CONFORMATIONAL DYNAMICS; CONFORMATIONAL TRANSITIONS; OXYFERRYL INTERMEDIATE; PHYSICO-CHEMICAL MECHANISMS; SEQUENTIAL ORDERING;

ENZYMES;

2 OXOGLUTARIC ACID; BACTERIAL ENZYME; PROTEIN ALKB; UNCLASSIFIED DRUG; ALKB PROTEIN, E COLI; ALPHA-KETOGLUTARIC ACID; BACTERIAL DNA; ESCHERICHIA COLI PROTEIN; LIGAND; MIXED FUNCTION OXIDASE; MUTANT PROTEIN; SUCROSE;

ARTICLE; BINDING AFFINITY; BIOPHYSICS; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROXYLATION; NUCLEIC ACID STRUCTURE; NUCLEOTIDE RECOGNITION LID; OXIDATION; PROTEIN FUNCTION; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE ANALYSIS; ALKYLATION; BIOCATALYSIS; CHEMISTRY; CIRCULAR DICHROISM; DNA REPAIR; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; KINETICS; METABOLISM; MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION;

ALKYLATION; BIOCATALYSIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; DNA REPAIR; DNA, BACTERIAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KETOGLUTARIC ACIDS; KINETICS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MIXED FUNCTION OXYGENASES; MUTANT PROTEINS; MUTATION; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; SUCROSE;

EID: 84908190413     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.575647     Document Type: Article

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