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Literature summary for 3.4.11.1 extracted from

  • Gardiner, D.L.; Trenholme, K.R.; Skinner-Adams, T.S.; Stack, C.M.; Dalton, J.P.
    Overexpression of leucyl aminopeptidase in Plasmodium falciparum parasites. Target for the antimalarial activity of bestatin (2006), J. Biol. Chem., 281, 1741-1745.
    View publication on PubMed

Application

Application Comment Organism
pharmacology the enzyme is a target for the antimalarial activity of inhibitor bestatin Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, overexpression of the full-length gene in parasite cytosol, transgenic parasites are more resistant to bestatin Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
bestatin
-
Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Plasmodium falciparum 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
65000
-
x * 65000, recombinant enzyme, SDS-PAGE, x * 67831, sequence calculation Plasmodium falciparum
67831
-
x * 65000, recombinant enzyme, SDS-PAGE, x * 67831, sequence calculation Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Plasmodium falciparum the enzyme is important in the generation and regulation of free amino acids that are used in protein anabolism and for maintaining osmotic stability within the infected erythrocyte, enzyme inhibition, e.g. by bestatin, blocks intraerythrocytic development of malaria parasites ?
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
clone D10 of isolate FC27
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alanyl-7-amido-4-methylcoumarin + H2O
-
Plasmodium falciparum alanine + 7-amino-4-methylcoumarin
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
-
Plasmodium falciparum L-leucine + 7-amino-4-methylcoumarin
-
?
additional information the enzyme is important in the generation and regulation of free amino acids that are used in protein anabolism and for maintaining osmotic stability within the infected erythrocyte, enzyme inhibition, e.g. by bestatin, blocks intraerythrocytic development of malaria parasites Plasmodium falciparum ?
-
?

Subunits

Subunits Comment Organism
? x * 65000, recombinant enzyme, SDS-PAGE, x * 67831, sequence calculation Plasmodium falciparum

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the peptidase family M17 Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Plasmodium falciparum