Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex

Journal of Biological Chemistry

Volumn 284, Issue 48, 2009, Pages 33122-33129

  Kale, Sachin ^a   Jordan, Frank ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AS-LIGANDS; BIOCHEMICAL STUDIES; BRANCH POINTS; CONFORMATIONAL ENSEMBLE; CONSERVED RESIDUES; COOPERATIVITY; ENZYME CATALYSIS; MULTIENZYME COMPLEXES; MULTIPLE MODES; NON-CATALYTIC; PYRUVATES; RATE DETERMINING STEP; THIAMIN DIPHOSPHATE-DEPENDENT ENZYMES;

CATALYSIS; CATALYSTS; COMMUNICATION; ESCHERICHIA COLI;

ENZYMES;

2 OXOACID DEHYDROGENASE; ASPARAGINE; DIHYDROLIPOAMIDE DEHYDROGENASE; GLYCINE; PYRUVATE DEHYDROGENASE; PYRUVATE DEHYDROGENASE COMPLEX;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME REGULATION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STEADY STATE; TEMPERATURE;

BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CIRCULAR DICHROISM; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PYRUVATE DEHYDROGENASE COMPLEX; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 70450245183     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.065508     Document Type: Article

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