Structure and reaction mechanism of phosphoethanolamine methyltransferase from the malaria parasite Plasmodium falciparum: An antiparasitic drug target

Journal of Biological Chemistry

Volumn 287, Issue 2, 2012, Pages 1426-1434

  Lee, Soon Goo ^a   Kim, Youngchang ^b   Alpert, Tara D ^a   Nagata, Akina ^a,c   Jez, Joseph M ^a  

^a WASHINGTON UNIVERSITY   (United States)

^b ARGONNE NATIONAL LABORATORY   (United States)

^c KNOX COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE ARCHITECTURE; ACTIVE SITE RESIDUES; ANTIPARASITIC DRUGS; FUNCTIONAL CHARACTERIZATION; ISOTHERMAL TITRATION CALORIMETRY; KINETIC ANALYSIS; LIGAND BINDING; MALARIA PARASITE; MALARIAL PARASITES; METABOLIC FUNCTION; METHYLTRANSFERASES; MULTI DOMAINS; NORMAL GROWTH; PHOSPHOCHOLINE; PHOSPHOETHANOLAMINE; PLASMODIUM FALCIPARUM; PROTEIN CRYSTALLOGRAPHY; REACTION MECHANISM; RESOLUTION STRUCTURE; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE; SINGLE-WAVELENGTH ANOMALOUS DISPERSIONS;

ALKYLATION; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY; LIGANDS; METHYLATION;

CRYSTAL STRUCTURE;

PHOSPHATIDYLETHANOLAMINE; PHOSPHOETHANOLAMINE METHYLTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; BIOGENESIS; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ISOTHERMAL TITRATION CALORIMETRY; KINETICS; NONHUMAN; PLASMODIUM FALCIPARUM; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS;

ADENOSINE; AMINO ACID SUBSTITUTION; ANTIMALARIALS; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DRUG DELIVERY SYSTEMS; ENZYME INHIBITORS; ETHANOLAMINES; HUMANS; KINETICS; MALARIA, FALCIPARUM; METHYLTRANSFERASES; MUTATION, MISSENSE; PHOSPHORYLCHOLINE; PLASMODIUM FALCIPARUM; PROTOZOAN PROTEINS;

NEMATODA; PISUM SATIVUM; PLASMODIUM FALCIPARUM;

EID: 84862974974     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.315267     Document Type: Article

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