Application | Comment | Organism |
---|---|---|
pharmacology | potential anti-malarial chemotherapy target | Plasmodium vivax |
Cloned (Comment) | Organism |
---|---|
expression of LAP in Escherichia coli strain BL21 | Plasmodium vivax |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Plasmodium vivax | 5829 | - |
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 Maximum [Da] | Comment | Organism |
---|---|---|---|
67800 | - |
x * 67800, recombinant enzyme, SDS-PAGE | Plasmodium vivax |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium vivax | A5K3U9 | - |
- |
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 | Comment | Organism |
---|---|---|
? | x * 67800, recombinant enzyme, SDS-PAGE | Plasmodium vivax |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
recombinant enzyme | Plasmodium vivax |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 11 | activity range, profile, overview | Plasmodium vivax |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is responsible for the catabolism of host hemoglobin | Plasmodium vivax |