Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg257/Lys 260, and unmasking of acid-base catalysis

Biological Chemistry

Volumn 390, Issue 11, 2009, Pages 1171-1183

  Urscher, Miriam ^a   Deponte, Marcel ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

Binuclear metallohydrolase; Catalysis; Glutathione; Glyoxalase system; Hydroxide formation; Malaria

Indexed keywords

ARGININE; GLUTATHIONE; GLYOXALASE; HYDROXIDE; HYDROXYACYLGLUTATHIONE HYDROLASE; LYSINE; METAL; SODIUM CHLORIDE;

ACIDITY; ALKALINITY; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ARGININE; BIOCATALYSIS; CATALYTIC DOMAIN; ENZYME INHIBITORS; GLUTATHIONE; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROXIDES; KINETICS; LYSINE; METALS; MODELS, MOLECULAR; MUTATION; PLASMODIUM FALCIPARUM; SALTS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; THIOLESTER HYDROLASES;

PLASMODIUM FALCIPARUM;

EID: 70349814275     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2009.127     Document Type: Article

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