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Description for Protein DPEP1

dipeptidase 1 (renal)
2 total interacting proteins;
Icon Book Platelet Evidence (proteome studies/others : 0/0)
(Not detected in platelets)
Summary:
DPEP1 (EC 3.4.13.11) is a kidney membrane enzyme that hydrolyzes a variety of dipeptides and is implicated in renal metabolism of glutathione and its conjugates, e.g., leukotriene D4 (Kozak and Tate, 1982 [PubMed 6122685]). DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics, such as penem and carbapenem (Campbell et al., 1984 [PubMed 6334084]). Earlier, beta-lactamase enzymes were thought to occur only in bacteria, where their probable function was in protecting the organisms against the action of beta-lactam antibiotics. These antibiotics exhibit selective toxicity against bacteria but virtual inertness against many eukaryotic cells (Adachi et al., 1990 [PubMed 2303490]).[supplied by OMIM] (PubMed Links)
Domains and Motifs:
  • SP: Signal Peptide
    • Gene Ontology:
    Gene Ontology Annotations
    KEGG - Enzyme ID(s):
    3.4.13.19
    KEGG - Orthology:
    K01273
    KEGG - Pathway(s):
    None Available
    Nomenclature / Alternative Names:
    Dipeptidase 1, renal; Dehydropeptidase 1; Microsomal dipeptidase; RDP; MDP
    Approved Symbol:
    DPEP1
    (De-) Phosphorylations:
    Total (de-) phosphorylation sites: 0
    No human (de-) phosphorylation sites; No platelet phosphorylation sites
    Phosphorylation Targets:
    Total phosphorylation targets: 0
    Human phosphorylation targets: 0;Predicted platelet targets: 0
    		Protein Characteristics:
    Isoform-specific Information
    Icon DrugsAssociated Drugs (DrugBank Accession):

  • Cilastatin(db)

    Associated Genetic Diseases:

    None Available
    		• Predicted Transmembrane Domains:
  • Isoform 2 : 0
  • Isoform 1 : 0
    • Additional Identifiers:

    HPRD: 01563 Entrez Gene ID: 1800 OMIM ID: 179780 Swissprot Accession: P16444;