The M17 leucine aminopeptidase of the malaria parasite Plasmodium falciparum: Importance of active site metal ions in the binding of substrates and inhibitors

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5435-5439

  Maric, Selma ^a   Donnelly, Sheila M ^a   Robinson, Mark W ^a   Skinner Adams, Tina ^b   Trenholme, Katharine R ^b   Gardiner, Donald L ^b   Dalton, John P ^a,e   Stack, Colin M ^a,c   Lowther, Jonathan ^a,d  

^a UNIVERSITY OF TECHNOLOGY SYDNEY   (Australia)

^b QIMR BERGHOFER MEDICAL RESEARCH INSTITUTE   (Australia)

^c UNIVERSITY OF WESTERN SYDNEY   (Australia)

^d UNIVERSITY OF EDINBURGH   (United Kingdom)

^e MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANTIMALARIAL ACTIVITY; CATALYTIC EFFICIENCIES; CONCENTRATION OF; CYTOSOLIC COMPARTMENTS; DIVALENT METAL CATIONS; DIVALENT METAL ION; IN-VITRO; LEUCINE AMINOPEPTIDASE; MALARIA PARASITE; METAL ION BINDING; METAL-BINDING SITES; MODE OF BINDING; PARASITE-; PEPTIDE SUBSTRATES; PLASMODIUM FALCIPARUM; PROTEIN SYNTHESIS; TIGHT BINDING;

AMINES; AMINO ACIDS; BINDING ENERGY; ENZYME ACTIVITY; ENZYMES; MANGANESE; MANGANESE COMPOUNDS; METAL IONS; METAL RECOVERY; METALS; ORGANIC ACIDS; TRACE ANALYSIS; ZINC;

BINDING SITES;

BESTATIN; EXOPEPTIDASE; M17 LEUCINE AMINOPEPTIDASE; MAGNESIUM ION; MANGANESE; METAL ION; RECOMBINANT ENZYME; RECOMBINANT M17 LEUCINE AMINOPEPTIDASE; UNCLASSIFIED DRUG; ZINC ION;

ANIMAL CELL; ANTIMALARIAL ACTIVITY; ARTICLE; BINDING SITE; CELL CULTURE; CONTROLLED STUDY; DRUG PROTEIN BINDING; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME SUBSTRATE; IN VITRO STUDY; INSECT CELL; MALARIA; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL;

ANIMALS; BINDING SITES; CATALYTIC DOMAIN; ENZYME INHIBITORS; KINETICS; LEUCYL AMINOPEPTIDASE; METALS; PLASMODIUM FALCIPARUM; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

PLASMODIUM FALCIPARUM;

EID: 67049154265     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9003638     Document Type: Article

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