3.4.11.9	evolution	enzyme PepP belongs to the family of proline-specific aminopeptidases	753399	
3.4.11.9	evolution	enzyme TgAPP is a member of the M24 prolyl aminopeptidase family	-, 754986	
3.4.11.9	evolution	pepP encodes an enzyme belonging to the aminopeptidases P (APPro) family, a type of metalloprotease that catalyzes the removal of the N-terminal residue from a polypeptide that has proline as the second residue. Enzyme PepP is highly conserved in all Pseudomonas aeruginosa genomes sequenced to date and has high genetic similarity with enzymes from other Pseudomonas species (82.4%-100% identity)	753683	
3.4.11.9	evolution	the enzyme belongs to the M24B subfamily of aminoproteases	-, 755354	
3.4.11.9	evolution	the enzyme TvMP50 belong to the aminopeptidase P-like metalloproteinase subfamily A/B, family M24 of clan MG, Parabasalia group. The Parabasalia group contains two protein lineages with a pita bread fold; the ancestral monomeric group 1 is probably derived from an ancestral dimeric aminopeptidase P-type enzyme, and group 2 has a probable dimeric kind of ancestral eukaryotic prolidase lineage. Phylogenetic analysis, overview	754700	
3.4.11.9	malfunction	deletion of TgAPP gene in the parasite through a CRISPR/Cas9 system results in inhibition of growth indicating the importance of TgAPP	-, 754986	
3.4.11.9	malfunction	in 2 families with an nephronophthisis-like phenotype, homozygous frameshift and splice-site mutations, respectively, are detected in the X-prolyl aminopeptidase 3 gene	709273	
3.4.11.9	malfunction	suppression of zebrafish xpnpep3 phenocopied the developmental phenotypes of ciliopathy morphants, and this effect is rescued by human XPNPEP3 that is devoid of a mitochondrial localization signal, suggesting that the protein might also have mitochondrial-independent activity	709273	
3.4.11.9	malfunction	Xpnpep1 knockout mice display severe growth retardation, microcephaly, and modest lethality. Imino-oligopeptide excretion is observed in urine samples from APP1-deficient mice	731249	
3.4.11.9	metabolism	four metalloaminopeptidases (MAPs) play a role in peptide turnover in Pf parasites: leucyl aminopeptidase (PfA-M17), alanyl aminopeptidase (PfA-M1), aspartyl aminopeptidase (PfM18AAP), and aminopeptidase P (PfAPP). The substrate profile shows that PfAPP has the capacity to catalyze the removal of any N-terminal amino acid residue from peptides with a P1' proline, and that the other MAPs in Plasmodium falciparum are unable to perform this function	752716