EC |
3.4.13.21 |
Accepted name: |
dipeptidase E |
Reaction: |
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 |
Other name(s): |
aspartyl dipeptidase; peptidase E; PepE gene product (Salmonella typhimurium) |
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: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB |
References: |
1. |
Haakansson, 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 (2000) 14097–14102. [DOI] [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 (2000) 2536–2543. [DOI] [PMID: 10762256] |
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[EC 3.4.13.21 created 2001] |
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