Function and Biology Details
Reaction catalysed:
Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase S15, X-Pro dipeptidyl-peptidase
- Xaa-Pro dipeptidyl-peptidase, C-terminal
- Alpha/Beta hydrolase fold
- Galactose-binding-like domain superfamily
- Xaa-Pro dipeptidyl-peptidase-like domain
- PepX, N-terminal domain superfamily
- X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain
- Homing endonuclease
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Xaa-Pro dipeptidyl-peptidase (preferred)
PDBe Complex ID:
PDB-CPX-176801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xaa-Pro dipeptidyl-peptidase
Molecule details ›
Chain: A
Length: 813 amino acids
Theoretical weight: 92.64 KDa
Source organism: Lactobacillus helveticus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 813 amino acids
Theoretical weight: 92.64 KDa
Source organism: Lactobacillus helveticus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q59485 (Residues: 1-793; Coverage: 100%)
Sequence domains:
