How dihydrofolate reductase facilitates protonation of dihydrofolate

Journal of the American Chemical Society

Volumn 125, Issue 29, 2003, Pages 8718-8719

  Rod, Thomas H ^a   Brooks III, Charles L ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE; DIHYDROFOLIC ACID;

ACCURACY; ARTICLE; CALCULATION; CATALYSIS; CHEMICAL REACTION; CRYSTALLOGRAPHY; ENERGY TRANSFER; ENZYME ANALYSIS; MOLECULAR INTERACTION; NONHUMAN; PROTON TRANSPORT; REACTION ANALYSIS;

CATALYSIS; FOLIC ACID; KINETICS; MODELS, MOLECULAR; PROTONS; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS;

EID: 0038298137     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja035272r     Document Type: Article

References (23)

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18. See Supporting Information for more details.
19. See also Supporting Information.
20. 2F pterine ring.
21. We find, on the basis of averages energies, that the closed conformation is more stable by ∼20 kcal/mol. This is a large number, but generally speaking we cannot expect to get accurate conformational energy differences by this method.
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23. 2F. The enzyme is therefore likely to sample other parts of configuration space when Asp27 is protonated.