MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

Homo sapiens: Dipeptidase 2: DPEP2
Dipeptidase 1: DPEP1
Rattus norvegicus: dehydropeptidase IInferred from experiment: DPEP1

Supersedes EC number:

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.

Instance reaction:
L-glutamyl-L-glutamate + H2O → 2 L-glutamate (

Enzyme Commission Primary Name: membrane dipeptidase

Enzyme Commission Synonyms: renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase (ambiguous), aminodipeptidase, dipeptide hydrolase (ambiguous), dipeptidyl hydrolase (ambiguous), nonspecific dipeptidase, glycosyl-phosphatidylinositol-anchored renal dipeptidase, MDP

Taxonomic Range: Fungi, Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -21.005234Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19.

Citations: [Campbell66, Kropp82, Hooper90 ]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reaction of [a dipeptide + H2O → 2 a standard α amino acid] (
i1: L-glutamyl-L-glutamate + H2O → 2 L-glutamate (

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O14124, UniProt:RELATED-TO:P16444, UniProt:RELATED-TO:P22412, UniProt:RELATED-TO:P31428, UniProt:RELATED-TO:P31429, UniProt:RELATED-TO:P31430, UniProt:RELATED-TO:Q43986

Revised 16-Mar-2011 by Caspi R, SRI International


Campbell66: Campbell BJ, Lin YC, Davis RV, Ballew E (1966). "The purification and properties of a particulate renal dipeptidase." Biochim Biophys Acta 118(2);371-86. PMID: 5961612

Hooper90: Hooper NM, Keen JN, Turner AJ (1990). "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme." Biochem J 265(2);429-33. PMID: 2137335

Kropp82: Kropp H, Sundelof JG, Hajdu R, Kahan FM (1982). "Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase." Antimicrob Agents Chemother 22(1);62-70. PMID: 7125632

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 Thu Nov 26, 2015, biocyc11.