Kinetic and structural characterization of dihydrofolate reductase from Streptococcus pneumoniae

Biochemistry

Volumn 49, Issue 1, 2010, Pages 195-206

  Lee, Jeeyeon ^a   Yennawar, Neela H ^b   Gam, Jongsik ^a   Benkovic, Stephen J ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BACTERIAL INFECTIONS; BACTERIAL SOURCE; BINDING PARAMETER; CATALYTIC RESIDUE; CRITICAL ELEMENTS; CRITICAL ISSUES; DIHYDROFOLATE REDUCTASE; DRUG RESISTANCE; E. COLI; HYDRIDE TRANSFERS; HYDROGEN BONDING NETWORK; HYDROXYL GROUPS; KINETIC CHARACTERIZATION; KINETIC PROPERTIES; PH DEPENDENCE; RATE LIMITING; RATE-LIMITING STEPS; SEQUENCE ANALYSIS; SIDE CHAINS; STEADY-STATE KINETICS; STREPTOCOCCUS PNEUMONIAE; STRUCTURAL CHARACTERIZATION; STRUCTURAL DATA; TETRAHYDROFOLATES; TRIMETHOPRIM; WATER MOLECULE; X-RAY STRUCTURE;

AMINO ACIDS; CARBOXYLATION; ESCHERICHIA COLI; HYDROGEN BONDS; ORGANIC ACIDS; REACTION KINETICS; STRUCTURAL ANALYSIS;

BACTERIOLOGY;

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; LEUCINE; METHOTREXATE; MUTANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRIMETHOPRIM;

ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL STRAIN; CRYSTALLIZATION; DISSOCIATION CONSTANT; DRUG TARGETING; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; HYDROGEN BOND; MUTANT; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; STEADY STATE; STREPTOCOCCUS PNEUMONIAE; THERMODYNAMICS;

AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; G-QUADRUPLEXES; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; STREPTOCOCCUS PNEUMONIAE; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS; TRIMETHOPRIM; TRIMETHOPRIM RESISTANCE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; STREPTOCOCCUS PNEUMONIAE;

EID: 73449112664     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901614m     Document Type: Article

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