DPEP1

Dipeptidase 1 (renal)
PDB rendering based on 1itq.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1itq​, 1itu​
Identifiers
Symbols	DPEP1 ; RDP; MBD1; MDP
External IDs	Template:OMIM5 Template:MGI HomoloGene: 80192
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Dipeptidase 1 (renal), also known as DPEP1, is a human gene.

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). DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics, such as penem and carbapenem (Campbell et al., 1984). 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).[supplied by OMIM]

Further reading

• 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.CS1 maint: Multiple names: authors list (link)
• Adachi H, Katayama T, Inuzuka C; et al. (1990). "Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form". J. Biol. Chem. 265 (25): 15341–5. PMID 2168407.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Adachi H, Tawaragi Y, Inuzuka C; et al. (1990). "Primary structure of human microsomal dipeptidase deduced from molecular cloning". J. Biol. Chem. 265 (7): 3992–5. PMID 2303490.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Adachi H, Kubota I, Okamura N; et al. (1989). "Purification and characterization of human microsomal dipeptidase". J. Biochem. 105 (6): 957–61. PMID 2768222.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Austruy E, Jeanpierre C, Antignac C; et al. (1993). "Physical and genetic mapping of the dipeptidase gene DPEP1 to 16q24.3". Genomics. 15 (3): 684–7. doi:10.1006/geno.1993.1126. PMID 7682195.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Satoh S, Ohtsuka K, Keida Y; et al. (1994). "Gene structural analysis and expression of human renal dipeptidase". Biotechnol. Prog. 10 (2): 134–40. PMID 7764673.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Adachi H, Katayama T, Nakazato H, Tsujimoto M (1993). "Importance of Glu-125 in the catalytic activity of human renal dipeptidase". Biochim. Biophys. Acta. 1163 (1): 42–8. PMID 8097406.CS1 maint: Multiple names: authors list (link)
• Satoh S, Kusunoki C, Konta Y; et al. (1993). "Cloning and structural analysis of genomic DNA for human renal dipeptidase". Biochim. Biophys. Acta. 1172 (1–2): 181–3. PMID 8439558.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Satoh S, Keida Y, Konta Y; et al. (1993). "Purification and molecular cloning of mouse renal dipeptidase". Biochim. Biophys. Acta. 1163 (3): 234–42. PMID 8507661.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kera Y, Liu Z, Matsumoto T; et al. (1999). "Rat and human membrane dipeptidase: tissue distribution and developmental changes". Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 123 (1): 53–8. PMID 10425712.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nitanai Y, Satow Y, Adachi H, Tsujimoto M (2002). "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis". J. Mol. Biol. 321 (2): 177–84. PMID 12144777.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• McIver CM, Lloyd JM, Hewett PJ, Hardingham JE (2004). "Dipeptidase 1: a candidate tumor-specific molecular marker in colorectal carcinoma". Cancer Lett. 209 (1): 67–74. doi:10.1016/j.canlet.2003.11.033. PMID 15145522.CS1 maint: Multiple names: authors list (link)
• Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMID 15340161.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)