EC Number   |
General Information |
Reference |
|---|
   3.4.11.9 | more |
analysis of structure-function relationship of aminopeptidase P, structure modelling, overview. A loop extending from the active site is important for specific large-substrate binding, and this non-conserved surface loop is also critical for Pseudomonas aeruginosa virulence. The extended substrate binding site is identified to be responsible for virulence-related protein recognition. |
753683 |
| 3.4.11.9 | more |
Caenorhabditis elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases |
753579 |
| 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 | 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 | physiological function |
eukaryotic aminopeptidase P1 (APP1) is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are resistant to cleavage by most peptidases, role for APP-1 is in the breakdown of imino-peptides generated during protein catabolism |
753579 |
| 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 |
| 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 | more |
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities |
754956 |
| 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 |
