Energy landscape of the michaelis complex of lactate dehydrogenase: Relationship to catalytic mechanism

Biochemistry

Volumn 53, Issue 11, 2014, Pages 1849-1857

  Peng, Huo Lei ^a   Deng, Hua ^a   Dyer, R Brian ^b   Callender, Robert ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b EMORY UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; CATALYSIS; ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN BONDS; ISOTOPES; PHASE SPACE METHODS; QUANTUM CHEMISTRY;

ACTIVE SITE RESIDUES; CATALYTIC EFFICIENCIES; CATALYTIC MECHANISMS; CONFORMATIONAL SUBSTATES; LACTATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDES; REACTION COORDINATES; STRUCTURE ACTIVITY RELATIONSHIPS;

CONFORMATIONS;

LACTATE DEHYDROGENASE; LACTIC ACID; MUTANT PROTEIN; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENERGY; ENERGY LANDSCAPE; ENZYME ACTIVITY; ENZYME CHEMISTRY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME STRUCTURE; HYDROGEN BOND; INFRARED SPECTROSCOPY; MICHAELIS COMPLEX; POLARIZATION; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ANIMALS; CATALYSIS; CATALYTIC DOMAIN; ENERGY METABOLISM; HYDRO-LYASES; NAD; PYRUVIC ACID; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STOCHASTIC PROCESSES; SWINE;

EID: 84897045920     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500215a     Document Type: Article

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