Role of the occluded conformation in bacterial dihydrofolate reductases

Biochemistry

Volumn 53, Issue 29, 2014, Pages 4761-4768

  Behiry, Enas M ^a   Luk, Louis Y P ^a   Matthews, Stella M ^a   Loveridge, E Joel ^a   Allemann, Rudolf K ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ESCHERICHIA COLI; HYDROGEN BONDS;

CATALYTIC CYCLES; DIHYDROFOLATE REDUCTASE; HYDRIDE TRANSFERS; HYDROGEN BOND DONORS; KINETIC PATHWAY; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATES; RATE DETERMINING STEP; RATE-LIMITING STEPS;

CONFORMATIONS;

DIHYDROFOLATE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; BACTERIAL PROTEIN; FOLIC ACID ANTAGONIST;

ARTICLE; CATALYSIS; ENZYME CONFORMATION; HYDROGEN BOND; MORITELLA; MORITELLA PROFUNDA; NONHUMAN; PH; PRIORITY JOURNAL; STEADY STATE; ANTAGONISTS AND INHIBITORS; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; KINETICS; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

BACTERIAL PROTEINS; BIOCATALYSIS; ENZYME STABILITY; ESCHERICHIA COLI; FOLIC ACID ANTAGONISTS; KINETICS; MODELS, MOLECULAR; MORITELLA; MUTAGENESIS, SITE-DIRECTED; NADP; OXIDATION-REDUCTION; PROTEIN CONFORMATION; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 84905046896     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500507v     Document Type: Article

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