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, alanyl aminopeptidase
- Aminopeptidase N-like , N-terminal domain superfamliy
- Peptidase M1, alanyl aminopeptidase, C-terminal
- Peptidase M1, alanyl aminopeptidase, C-terminal domain superfamily
- Alanyl aminopeptidase, Ig-like domain superfamily
- Peptidase M1, alanyl aminopeptidase, Ig-like fold
- Peptidase M4/M1, CTD superfamily
2 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Aminopeptidase N (preferred)
PDBe Complex ID:
PDB-CPX-138200 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase N
Molecule details ›
Chain: A
Length: 870 amino acids
Theoretical weight: 99.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 870 amino acids
Theoretical weight: 99.03 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P04825 (Residues: 1-870; Coverage: 100%)
Sequence domains:
- Peptidase M1 N-terminal domain
- Peptidase family M1 domain
- Domain of unknown function (DUF3458) Ig-like fold
- Domain of unknown function (DUF3458_C) ARM repeats
