Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: Comparison of wild-type protein and active-site mutant D27E

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 12, 2013, Pages 2782-2794

  Ohmae, Eiji ^a   Miyashita, Yurina ^a   Tate, Shin Ichi ^a   Gekko, Kunihiko ^a,e   Kitazawa, Soichiro ^b   Kitahara, Ryo ^b   Kuwajima, Kunihiro ^c,d  

^a HIROSHIMA UNIVERSITY   (Japan)

^b RITSUMEIKAN UNIVERSITY   (Japan)

^c OKAZAKI INSTITUTE FOR INTEGRATIVE BIOSCIENCE   (Japan)

^d GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

^e HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Active site mutation; Cavity and hydration; Dihydrofolate reductase; Enzyme function; High pressure; Solvent effect

Indexed keywords

BARIUM CHLORIDE; CATION; DIHYDROFOLATE REDUCTASE; FOLIC ACID; LITHIUM CHLORIDE; NITROGEN 15; POTASSIUM CHLORIDE; PROTON; SODIUM CHLORIDE;

ARTICLE; BINDING SITE; CHEMICAL ENVIRONMENT; COMPARATIVE STUDY; COMPETITIVE INHIBITION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; FLUORESCENCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HYDRATION; MUTANT; NONHUMAN; PH; PRESSURE; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLVENT EFFECT; WILD TYPE;

EID: 84887044394     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.09.024     Document Type: Article

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