Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 14, 2005, Pages 5032-5037

  McElheny, Dan ^a,b   Schnell, Jason R ^a,c   Lansing, Jonathan C ^a   Dyson, H Jane ^a   Wright, Peter E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Enzyme catalysis; Hydride transfer; NMR relaxation

Indexed keywords

DIHYDROFOLATE REDUCTASE; FOLIC ACID; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; NONHUMAN; PRIORITY JOURNAL; THERMODYNAMICS;

BIOPHYSICS; CATALYSIS; CATALYTIC DOMAIN; ESCHERICHIA COLI; FOLIC ACID; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NADP; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS;

EID: 17044401342     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0500699102     Document Type: Article

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