Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.11.1 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
Search for more literature for 3.4.11.1

Application

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

Cloned(Commentary)

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

Inhibitors

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

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ highly activating Plasmodium vivax
Mg2+ highly activating Plasmodium vivax
Mn2+ highly activating Plasmodium vivax
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
Ni2+ highly activating Plasmodium vivax
Zn2+ highly activating Plasmodium vivax

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Plasmodium vivax A5K3U9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
L-leucine-4-methylcoumaryl-7-amide + H2O best synthetic substrate Plasmodium vivax L-leucine + 7-amino-4-methylcoumarine
-
 ?
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
-
 ?
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

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

Synonyms

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

pH Optimum

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

pH Range

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

General Information

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