Dipeptidase E

{{Infobox enzyme | Name = Dipeptidase E | EC_number = 3.4.13.21 | CAS_number = | GO_code = | image = | width = | caption = }} {{Infobox nonhuman protein | UniProt=P36936 | Symbol=PepE | Organism=Salmonella typhimurium }} '''Dipeptidase E''' ({{EC number|3.4.13.21}}, ''aspartyl dipeptidase'', ''peptidase E'', ''PepE gene product (Salmonella typhimurium)'') is an enzyme.<ref>{{cite journal | vauthors = Håkansson K, Wang AH, Miller CG | title = The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 26 | pages = 14097–102 | date = December 2000 | pmid = 11106384 | pmc = 18877 | doi = 10.1073/pnas.260376797 | bibcode = 2000PNAS...9714097H | doi-access = free }}</ref><ref>{{cite journal | vauthors = Lassy RA, Miller CG | title = Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase | journal = Journal of Bacteriology | volume = 182 | issue = 9 | pages = 2536–43 | date = May 2000 | pmid = 10762256 | pmc = 111318 | doi = 10.1128/jb.182.9.2536-2543.2000 }}</ref> This enzyme catalyses the following chemical 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

A free carboxy group is not absolutely required in the substrate.

== References == {{reflist}}

== External links == * {{MeshName|Dipeptidase+E}}

Category:EC 3.4.13