Function and Biology Details
Reaction catalysed:
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase M1, alanine aminopeptidase/leukotriene A4 hydrolase
- Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal
- Aminopeptidase N-like , N-terminal domain superfamliy
- Aminopeptidase, leukotriene A4 hydrolase-like
- Peptidase M1, LTA-4 hydrolase/aminopeptidase, C-terminal domain superfamily
- Armadillo-type fold
- Peptidase M4/M1, CTD superfamily
- Peptidase M1, membrane alanine aminopeptidase
1 more domain
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Aminopeptidase N (preferred)
PDBe Complex ID:
PDB-CPX-182147 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase N
Molecule details ›
Chains: A, B, C, D
Length: 605 amino acids
Theoretical weight: 68.67 KDa
Source organism: Colwellia psychrerythraea 34H
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 605 amino acids
Theoretical weight: 68.67 KDa
Source organism: Colwellia psychrerythraea 34H
Expression system: Escherichia coli
UniProt:
- Canonical:
Q7WVY1 (Residues: 25-629; Coverage: 100%)
Sequence domains:
Structure domains:
