Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: Mutational effects on hydride transfer rates

Biochemistry

Volumn 41, Issue 42, 2002, Pages 12618-12628

  Ravi Rajagopalan, P T ^a   Lutz, Stefan ^a,b   Benkovic, Stephen J ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b EMORY UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MUTANTS;

CATALYSIS; ENZYMES; HYDRIDES; MUTAGENESIS;

BIOCHEMISTRY;

DIHYDROFOLATE REDUCTASE;

ALLOSTERISM; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; DISSOCIATION CONSTANT; ENZYME ACTIVE SITE; ENZYME BINDING; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; QUANTUM CHEMISTRY; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; COMPUTATIONAL BIOLOGY; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; FLUORESCENCE RESONANCE ENERGY TRANSFER; GLYCINE; HYDROGEN; KINETICS; LIGANDS; METHIONINE; MUTAGENESIS, SITE-DIRECTED; NADP; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS;

EID: 0037159205     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026369d     Document Type: Article

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