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 analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Peptidase E (preferred)
PDBe Complex ID:
PDB-CPX-153263 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase E
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 28.6 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Peptidase family S51
Structure domains: Rossmann fold
Length: 265 amino acids
Theoretical weight: 28.6 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P36936 (Residues: 2-229; Coverage: 100%)
Sequence domains: Peptidase family S51
Structure domains: Rossmann fold
