Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 3.4.13.21

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.4.13.21

Enzymes and Genes:
peptidase E, a dipeptidase where amino-terminal residue is aspartate Inferred from experiment : pepE ( Escherichia coli K-12 substr. MG1655 )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

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 Inferred 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: ?

Relationship Links: BRENDA:EC:3.4.13.21 , ENZYME:EC:3.4.13.21 , IUBMB-ExplorEnz:EC:3.4.13.21


References

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 SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC13B.