The dynamic energy landscape of dihydrofolate reductase catalysis

Science

Volumn 313, Issue 5793, 2006, Pages 1638-1642

  Boehr, David D ^a   McElheny, Dan ^a,b   Dyson, H Jane ^a   Wrightt, Peter E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ENGINEERING; CATALYSIS; CONFORMATIONS; ENZYME KINETICS; ESCHERICHIA COLI; HYDRIDES;

COFACTORS; ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE; HYDRIDE TRANSFER; LIGANDS;

ENZYMES;

DIHYDROFOLATE REDUCTASE; LIGAND;

CATALYSIS; COLIFORM BACTERIUM; ENZYME ACTIVITY; KINETICS; LIGAND; NUCLEAR MAGNETIC RESONANCE;

ARTICLE; DYNAMICS; ENERGY; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; STEADY STATE;

BINDING SITES; CATALYSIS; ESCHERICHIA COLI; KINETICS; LIGANDS; MODELS, MOLECULAR; NADP; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; TETRAHYDROFOLATE DEHYDROGENASE; TETRAHYDROFOLATES; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 33748781457     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1130258     Document Type: Article

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29. We thank J. Chung and G. Kroon for assistance with the NMR experiments, L. Tennant for technical assistance, and S. Benkovic for valuable discussions. This work was supported by NIH grants GM56879 and GM75995 and by the Skaggs Institute for Chemical Biology. D.D.B. was a recipient of a Canadian Institutes of Health Research postdoctoral fellowship. D.M. was supported by a postdoctoral fellowship from NIH.