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EC 3.4.13.21 Details
EC number
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)
Comment
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.
History
created 2001
EC Tree
3.4.13.1 created 1972, deleted 1978 [transferred to EC 3.4.13.11, deleted 1992]
3.4.13.2 created 1972, deleted 1978 [transferred to EC 3.4.13.11, deleted 1992]
3.4.13.6 created 1961 as EC 3.4.3.5, transferred 1972 to EC 3.4.13.6
3.4.13.8 created 1961 as EC 3.4.3.6, transferred 1972 to EC 3.4.13.8
3.4.13.10 created 1972, deleted 1992
3.4.13.11 created 1972, deleted 1992
3.4.13.13 created 1981, deleted 1992
3.4.13.14 created 1989, deleted 1992
3.4.13.15 created 1989, deleted 1992
3.4.13.16 created 1989, deleted 1992