Application | Comment | Organism |
---|---|---|
drug development | the enzyme represents a target for which antimalarials can be designed since metalloaminopeptidase inhibitors prevent the growth of the parasites in vitro and in vivo | Plasmodium falciparum |
Cloned (Comment) | Organism |
---|---|
His-tagged LAP expression in insect cells | Plasmodium falciparum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
bestatin | a metal-chelating inhibitor of M17 aminopeptidases with antimalarial activity, the type of metal ion present at site 1 influences the mode of binding by bestatin | Plasmodium falciparum | |
EDTA | - |
Plasmodium falciparum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | metal ion binding kinetics to the recombinant enzyme, metal ion occupying site 1 can influence enzyme substrate kinetics, overview | Plasmodium falciparum | |
0.35 | - |
L-leucine-4-methylcoumaryl-7-amide | pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2 | Plasmodium falciparum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Plasmodium falciparum | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | binds at metal site 1 | Plasmodium falciparum | |
Mg2+ | binds at metal site 1 | Plasmodium falciparum | |
Mn2+ | binds at metal site 1 | Plasmodium falciparum | |
additional information | the exopeptidase contains two metal-binding sites, a readily exchangeable site and a tight binding site. The enzyme retains activity when the metal ion is removed from site 1, while removal of metal ions from both sites results in an inactive apoenzyme that cannot be reactivated by the addition of divalent metal cations. The metal ion at site 1 is readily exchangeable with several divalent metal ions and displays a preference in the order of preference Zn2+, Mn2+, Co2+, Mg2+. While it is likely that native PfLAP contains a Zn2+ in site 2. the type of metal ion present at site 1 influences not only the catalytic efficiency of the enzyme for peptide substrates but also the mode of binding by bestatin, a metal-chelating inhibitor of M17 aminopeptidases with antimalarial activity | Plasmodium falciparum | |
Zn2+ | binds at metal sites 1 and 2 | Plasmodium falciparum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged LAP from insect cells by nickel affinity chromatography | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-leucine-4-methylcoumaryl-7-amide + H2O | - |
Plasmodium falciparum | L-leucine + 7-amino-4-methylcoumarine | - |
? | |
additional information | the type of metal ion present at site 1 influences the catalytic efficiency of the enzyme for peptide substrates | Plasmodium falciparum | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LAP | - |
Plasmodium falciparum |
M17 leucine aminopeptidase | - |
Plasmodium falciparum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Plasmodium falciparum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0094 | - |
L-leucine-4-methylcoumaryl-7-amide | pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2 | Plasmodium falciparum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Plasmodium falciparum |
General Information | Comment | Organism |
---|---|---|
physiological function | the M17 leucine aminopeptidase of the intraerythrocytic stages of the malaria parasite Plasmodium falciparum plays a role in releasing amino acids from host hemoglobin that are used for parasite protein synthesis, growth, and development | Plasmodium falciparum |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0027 | - |
L-leucine-4-methylcoumaryl-7-amide | pH 8.0, 37°C, recombinant enzyme in presence of Zn2+ and Mg2+, best ion combination at metal binding sites 1 and 2 | Plasmodium falciparum |