Strength of an interloop hydrogen bond determines the kinetic pathway in catalysis by Escherichia coli dihydrofolate reductase

Biochemistry

Volumn 37, Issue 18, 1998, Pages 6336-6342

  Miller, Grover Paul ^a   Benkovic, Stephen J ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME ANALYSIS; ENZYME KINETICS; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HYDROGEN BONDING; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TETRAHYDROFOLATE DEHYDROGENASE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032485865     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi973065w     Document Type: Article

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