EC 3.4.13.21 - Dipeptidase E

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IntEnz Enzyme Nomenclature
EC 3.4.13.21

Names

Accepted name:
dipeptidase E
Other names:
PepE gene product (Salmonella typhimurium)
aspartyl dipeptidase
peptidase E
Systematic name:

Reaction

Comments:

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0017165
UniProtKB/Swiss-Prot: (63) [show] [UniProt]

References

  1. Håkansson, K., Wang, A.H.J. and Miller, C.G.
    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]
  2. Lassy, R.A.L. and Miller, C.G.
    Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase.
    J. Bacteriol. 182: 2536-2543 (2000). [PMID: 10762256]

[EC 3.4.13.21 created 2001]