EC Number   |
General Information |
Reference |
|---|
   3.4.11.9 | metabolism |
the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803 contains 25 genes of aminopeptidases, among which only the sll0136 gene encodes a aminopeptidase P (PepP) |
753399 |
| 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 | more |
isozymes XPNPEP1 and -2 have comparable structural properties and similar substrate specificities |
754956 |
| 3.4.11.9 | more |
the active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P |
-, 755354 |
| 3.4.11.9 | more |
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-121) and a C-terminal domain (residues 122-349). The C-terminal domain, adopting a typical pitabread-fold, houses the metal binding active site. Residues Asp53, Arg55, and Tyr56 are part of the conserved DXRY motif, which is important for enzymatic activity, His193 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substrates. Residue His93 is expected to interact with the DXRY motif in the closed conformation and may also be involved in substrate binding, His281 is expected to be part of the proline binding pocket, and Arg298 is expected to interact with tripeptide and longer peptide substratesBoth His281 and Arg298 residues are found to be disordered in the Dr-smAPP structure. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P |
-, 755354 |
| 3.4.11.9 | more |
the protein adopts a two-domain structure typical of the M24B subfamily with an N-terminal domain (residues 1-123) and a C-terminal domain (residues 124-360). The C-terminal domain, adopting a typical pita-bread-fold, houses the metal binding active site. The active site includes the DXRY motif. Structure comparisons of small aminopeptidases-P |
755354 |
| 3.4.11.9 | more |
three-dimensional modeling of the Synechocystis sp. PCC6803 PepP protein, overview. The PepP amino acid residues Asp260, Asp271, His354, Glu385, and Glu415 are involved in the formation of the enzym's catalytic site |
753399 |
| 3.4.11.9 | more |
three-dimensional structure analysis and structure-function analysis, structure comparisons, overview |
752716 |
| 3.4.11.9 | more |
Trichomonas vaginalis metalloproteinase TvMP50 is a monomeric aminopeptidase P-like enzyme |
754700 |
