|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
|Homo sapiens:||Dipeptidase 2: DPEP2|
Dipeptidase 1: DPEP1
|Rattus norvegicus:||dehydropeptidase I: DPEP1|
Supersedes EC number: 22.214.171.124
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.
L-glutamyl-L-glutamate + H2O → 2 L-glutamate (126.96.36.199)
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
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -21.005234 [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.
Relationship Links: BRENDA:EC:188.8.131.52, ENZYME:EC:184.108.40.206, IUBMB-ExplorEnz:EC:220.127.116.11, 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
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
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