EC 184.108.40.206 - Dipeptidase E
IntEnz Enzyme Nomenclature
- Dipeptidase E catalyses 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.
A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed somewhat more slowly than dipeptides with free C-termini. No peptide larger than a C-blocked dipeptide is known to be a substrate. Asp-NH-Np is hydrolysed and is a convenient substrate for routine assay. The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. Belongs in peptidase family S51.
Links to other databases
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.Proc. Natl. Acad. Sci. USA 97: 14097-14102 (2000). [PMID: 11106384]
Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase.J. Bacteriol. 182: 2536-2543 (2000). [PMID: 10762256]
[EC 220.127.116.11 created 2001]