|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
|Escherichia coli K-12 substr. MG1655 :||peptidase E, a dipeptidase where amino-terminal residue is aspartate
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 39.271484 [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.
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
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