Function and Biology Details
Reaction catalysed:
Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Peptidase E (preferred)
PDBe Complex ID:
PDB-CPX-153262 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase E
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 24.79 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
Sequence domains: Peptidase family S51
Structure domains: Rossmann fold
Length: 229 amino acids
Theoretical weight: 24.79 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
- Canonical:
P36936 (Residues: 1-229; Coverage: 100%)
Sequence domains: Peptidase family S51
Structure domains: Rossmann fold
