3.4.13.21: dipeptidase E

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For detailed information about dipeptidase E, go to the full flat file.

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 =

Synonyms

alpha-aspartyl dipeptidase, Asp-specific dipeptidase, aspartyl dipeptidase, dipeptidase E, PepE, PepE gene product, Salmonella typhimurium, peptidase E

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.13 Dipeptidases

                3.4.13.21 dipeptidase E

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Results	in table
2909	AA Sequence
1	CAS Registry Number
5	Cloned(Commentary)
3	Crystallization (Commentary)
6	Inhibitors
3	KM Value [mM]
1	Metals/Ions
4	Molecular Weight [Da]
26	Organism
6	PDB ID
12	pH Optimum
1	pH Range
6	Protein Variants
5	Purification (Commentary)
1	Reaction
1	Reaction Type
26	Reference
3	Specific Activity [micromol/min/mg]
40	Substrates and Products (Substrate)
1	Subunits
24	Synonyms
9	Temperature Optimum [°C]
1	Temperature Stability [°C]
3	Turnover Number [1/s]

Reaction

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Reaction on EC 3.4.13.21 - dipeptidase E

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

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 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

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