MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: peptidase E, a dipeptidase where amino-terminal residue is aspartateInferred from experiment: pepE

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: dipeptidase E

Enzyme Commission Synonyms: aspartyl dipeptidase, peptidase E, PepE gene product (Salmonella typhimurium)

Taxonomic Range: Metazoa, Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): 39.271484Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Dipeptidase E catalyzes 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 to peptidase family S51.

Citations: [Hakansson00, Lassy00 ]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Hakansson00: Hakansson K, Wang AH, Miller CG (2000). "The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad." Proc Natl Acad Sci U S A 97(26);14097-102. PMID: 11106384

Lassy00: Lassy RA, Miller CG (2000). "Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase." J Bacteriol 182(9);2536-43. PMID: 10762256

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue Nov 24, 2015, biocyc11.