Structures of asymmetric complexes of human neuron specific enolase with resolved substrate and product and an analogous complex with two inhibitors indicate subunit interaction and inhibitor cooperativity

Journal of Inorganic Biochemistry

Volumn 111, Issue , 2012, Pages 187-194

  Qin, Jie ^a   Chai, Geqing ^a   Brewer, John M ^b   Lovelace, Leslie L ^a   Lebioda, Lukasz ^a  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

^b University of Georgia   (United States)

Author keywords

Active site cooperativity; Enolase; Heteroinhibition; Homodimer asymmetry

Indexed keywords

LACTIC ACID; MAGNESIUM; NEURON SPECIFIC ENOLASE; PHOSPHOENOLPYRUVATE; TARTRONIC ACID;

ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STRUCTURE; GLUCONEOGENESIS; GLYCOLYSIS; HUMAN;

BINDING, COMPETITIVE; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; GLYCERIC ACIDS; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PHOSPHOENOLPYRUVATE; PHOSPHOPYRUVATE HYDRATASE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TARTRONATES;

EID: 84861961492     PISSN: 01620134     EISSN: 18733344     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2012.02.011     Document Type: Article

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