Thermodynamic evaluation of ligand binding in the plant-like phosphoethanolamine methyltransferases of the parasitic nematode Haemonchus contortus

Journal of Biological Chemistry

Volumn 286, Issue 44, 2011, Pages 38060-38068

  Lee, Soon Goo ^a   Haakenson, William ^b   McCarter, James P ^b   Williams, D Jeremy ^b   Hresko, Michelle C ^b   Jez, Joseph M ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Divergence Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CAENORHABDITIS ELEGANS; CONFORMATIONAL CHANGE; DIPHENHYDRAMINE; ELEGANS; HEAT CAPACITY CHANGE; ISOTHERMAL TITRATION CALORIMETRY; KINETIC ANALYSIS; LIGAND BINDING; METHYLTRANSFERASES; N-TERMINALS; NACL CONCENTRATION; PHOSPHOCHOLINE; PHOSPHOETHANOLAMINE; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE; SEQUENCE ANALYSIS; SINGLE BINDING SITES; SURFACE AREA; THERAPEUTIC TARGETS; THERMODYNAMIC EVALUATION; VAN'T HOFF PLOTS;

CATALYSTS; SODIUM CHLORIDE;

ENZYMES;

AMODIAQUINE; DIPHENHYDRAMINE; METHYLTRANSFERASE; MILTEFOSINE; PHOSPHODIMETHYLETHANOLAMINE; PHOSPHOETHANOLAMINE; PHOSPHOETHANOLAMINE METHYLTRANSFERASE; PHOSPHOMONOMETHYLETHANOLAMINE; PHOSPHORYLCHOLINE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; SINEFUNGIN; SODIUM CHLORIDE; TACRINE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; HAEMONCHUS CONTORTUS; IC 50; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE ANALYSIS; THERMODYNAMICS;

ANIMALS; ANTIPARASITIC AGENTS; CALORIMETRY; CLONING, MOLECULAR; ENZYME INHIBITORS; HAEMONCHUS; INHIBITORY CONCENTRATION 50; KINETICS; LIGANDS; METHYLATION; METHYLTRANSFERASES; MODELS, CHEMICAL; PHOSPHORYLCHOLINE; TEMPERATURE; THERMODYNAMICS;

CAENORHABDITIS ELEGANS; HAEMONCHUS CONTORTUS; NEMATODA;

EID: 80055072963     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.290619     Document Type: Article

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