Role of Lys-12 in catalysis by triosephosphate isomerase: A two-part substrate approach

Biochemistry

Volumn 49, Issue 25, 2010, Pages 5377-5389

  Go, Maybelle K ^a   Koudelka, Astrid ^a   Amyes, Tina L ^a   Richard, John P ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLAMMONIUM; CATALYZED REACTIONS; COMPETITIVE INHIBITION; DIHYDROXYACETONE PHOSPHATE; ELIMINATION REACTION; ENOLATES; GLYCOLALDEHYDES; GROUND-STATE INTERACTIONS; METHYLGLYOXAL; MICHAELIS COMPLEX; MUTANT ENZYMES; MUTATION RESULTS; NEGATIVE CHARGE; SACCHAROMYCES CEREVISIAE; SIDE CHAINS; STABILIZING INTERACTIONS; TRANSITION STATE; TRIOSEPHOSPHATE ISOMERASE;

ALDEHYDES; CATALYSIS; ELECTRON TRANSITIONS; ENZYMES; ISOMERIZATION; ISOMERS; OXYGEN; SUBSTRATES; SUGAR (SUCROSE); TECHNOLOGICAL FORECASTING; YEAST;

GALLIUM ALLOYS;

LYSINE; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME INHIBITION; GENE MUTATION; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTON TRANSPORT; SACCHAROMYCES CEREVISIAE;

BASE SEQUENCE; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DNA PRIMERS; KINETICS; LYSINE; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; TRIOSE-PHOSPHATE ISOMERASE;

SACCHAROMYCES CEREVISIAE;

EID: 77953888039     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100538b     Document Type: Article

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