Dipeptidase E
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.13 Dipeptidases > 3.4.13.21 dipeptidase E
Dipeptidase E is a serine peptidase in family S51 that hydrolyses dipeptides Asp-Xaa; a free carboxy group is not absolutely required since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed somewhat more slowly than free-C-terminus dipeptides, no peptide larger than a C-blocked dipeptide is a substrate, Asp-NH-Np is a convenient assay substrate, the enzyme is most active near pH 7.0 and is not inhibited by diisopropyl fluorophosphate or phenylmethanesulfonyl fluoride; it does not act on peptides with N-terminal Glu, Asn or Gln and does not cleave isoaspartyl peptides. By digesting Asp-Xaa dipeptides it participates in cytosolic peptide catabolism. It is distributed across Eukaryota and Bacteria.
Dipeptidase E is a serine peptidase in family S51 that hydrolyses dipeptides Asp-Xaa; a free carboxy group is not absolutely required since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed somewhat more slowly than free-C-terminus dipeptides, no peptide larger than a C-blocked dipeptide is a substrate, Asp-NH-Np is a convenient assay substrate, the enzyme is most active near pH 7.0 and is not inhibited by diisopropyl fluorophosphate or phenylmethanesulfonyl fluoride; it does not act on peptides with N-terminal Glu, Asn or Gln and does not cleave isoaspartyl peptides. By digesting Asp-Xaa dipeptides it participates in cytosolic peptide catabolism. It is distributed across Eukaryota and Bacteria.
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