Function and Biology Details
Reaction catalysed:
Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
homo dodecamer (preferred)
Assembly name:
Vacuolar aminopeptidase 1 (preferred)
PDBe Complex ID:
PDB-CPX-147137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar aminopeptidase 1
Molecule details ›
Chain: A
Length: 514 amino acids
Theoretical weight: 57.16 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
Length: 514 amino acids
Theoretical weight: 57.16 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P14904 (Residues: 1-514; Coverage: 100%)
Sequence domains: Aminopeptidase I zinc metalloprotease (M18)
