Metabolic Modeling Tutorial
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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: 3.4.13.19

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

EC Number: 3.4.13.19

Enzymes and Genes:
Dipeptidase 1 : DPEP1 ( Homo sapiens )
Dipeptidase 2 : DPEP2 ( Homo sapiens )
dehydropeptidase I Inferred from experiment : DPEP1 ( Rattus norvegicus )

Supersedes EC number: 3.4.13.11

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.

Instance reaction:
L-glutamyl-L-glutamate + H2O → 2 L-glutamate (3.4.13.7)

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 Inferred 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: ?

Instance reaction of [a dipeptide + H2O → 2 a standard α amino acid] (3.4.13.18):
i1: L-glutamyl-L-glutamate + H2O → 2 L-glutamate (3.4.13.7)

Relationship Links: BRENDA:EC:3.4.13.19 , ENZYME:EC:3.4.13.19 , IUBMB-ExplorEnz:EC:3.4.13.19 , 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

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


References

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 SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13B.