release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
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
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
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
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
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
DNA and amino acid sequence determination and analysis, overexpression of the full-length gene in parasite cytosol, transgenic parasites are more resistant to bestatin
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
Characterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug development
Identification of phosphinate dipeptide analog inhibitors directed against the Plasmodium falciparum M17 leucine aminopeptidase as lead antimalarial compounds
The M17 leucine aminopeptidase of the malaria parasite Plasmodium falciparum: importance of active site metal ions in the binding of substrates and inhibitors