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Literature summary extracted from

  • Lee, J.Y.; Song, S.M.; Seok, J.W.; Jha, B.K.; Han, E.T.; Song, H.O.; Yu, H.S.; Hong, Y.; Kong, H.H.; Chung, D.I.
    M17 leucine aminopeptidase of the human malaria parasite Plasmodium vivax (2010), Mol. Biochem. Parasitol., 170, 45-48.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.11.1 pharmacology potential anti-malarial chemotherapy target Plasmodium vivax

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.1 expression of LAP in Escherichia coli strain BL21 Plasmodium vivax

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.1 1,10-phenanthroline 16% inhibition at 1 mM, 77% at 10 mM Plasmodium vivax
3.4.11.1 bestatin 17% inhibition at 0.01 mM, 88% at 0.1 mM Plasmodium vivax
3.4.11.1 Ca2+ inhibitory at 10 mM Plasmodium vivax
3.4.11.1 EDTA 38% inhibition at 1 mM, 97% at 10 mM Plasmodium vivax

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.1 cytosol
-
 Plasmodium vivax 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.1 Co2+ highly activating Plasmodium vivax
3.4.11.1 Mg2+ highly activating Plasmodium vivax
3.4.11.1 Mn2+ highly activating Plasmodium vivax
3.4.11.1 additional information metallo-exopeptidase, enzyme activity is dependent on divalent metal ions best activation at 0.1-1 mM metal ion. M17 family of metalloproteinase contains two metal-binding sites having different affinities for metal ions Plasmodium vivax
3.4.11.1 Ni2+ highly activating Plasmodium vivax
3.4.11.1 Zn2+ highly activating Plasmodium vivax

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.1 67800
-
 x * 67800, recombinant enzyme, SDS-PAGE Plasmodium vivax

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.1 additional information Plasmodium vivax M17 leucine aminopeptidase LAP is a cytosolic metallo-exopeptidase that catalyzes the removal of amino acids from the peptide generated in the process of hemoglobin degradation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.1 Plasmodium vivax A5K3U9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.1 L-arginine-4-methylcoumaryl-7-amide + H2O about 2% activity compared to L-leucyl-4-methylcoumaryl-7-amide Plasmodium vivax L-arginine + 7-amino-4-methylcoumarine
-
 ?
3.4.11.1 L-leucine-4-methylcoumaryl-7-amide + H2O best synthetic substrate Plasmodium vivax L-leucine + 7-amino-4-methylcoumarine
-
 ?
3.4.11.1 L-tyrosine-4-methylcoumaryl-7-amide + H2O 20% activity compared to L-leucyl-4-methylcoumaryl-7-amide Plasmodium vivax L-tyrosine + 7-amino-4-methylcoumarine
-
 ?
3.4.11.1 additional information M17 leucine aminopeptidase LAP is a cytosolic metallo-exopeptidase that catalyzes the removal of amino acids from the peptide generated in the process of hemoglobin degradation Plasmodium vivax ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.1 ? x * 67800, recombinant enzyme, SDS-PAGE Plasmodium vivax

Synonyms

EC Number Synonyms Comment Organism
3.4.11.1 LAP
-
 Plasmodium vivax
3.4.11.1 M17 leucine aminopeptidase
-
 Plasmodium vivax
3.4.11.1 More the enzyme belongs to the M17 family leucine aminopeptidases Plasmodium vivax

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.1 8.5
-
 recombinant enzyme Plasmodium vivax

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.11.1 7 11 activity range, profile, overview Plasmodium vivax

General Information

EC Number General Information Comment Organism
3.4.11.1 physiological function the enzyme is responsible for the catabolism of host hemoglobin Plasmodium vivax