Dipeptidase 1

Dipeptidase 1 (renal)
PDB rendering based on 1itq.
Available structures PDB 1ITQ, 1ITU
Identifiers
Symbols	DPEP1; MBD1; MDP; RDP
External IDs	OMIM: 179780 MGI: 94917 HomoloGene: 80192 GeneCards: DPEP1 Gene
EC number	3.4.13.19
Gene Ontology Molecular function • protein binding • peptidase activity • metalloexopeptidase activity • dipeptidyl-peptidase activity • dipeptidase activity • metal ion binding Cellular component • plasma membrane • apical plasma membrane • anchored to membrane • microvillus membrane • cell projection Biological process • proteolysis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1800	13479
Ensembl	ENSG00000015413	ENSMUSG00000019278
UniProt	P16444	Q3V175
RefSeq (mRNA)	NM_001128141.1	NM_007876.2
RefSeq (protein)	NP_001121613.1	NP_031902.2
Location (UCSC)	Chr 16: 89.68 – 89.7 Mb	Chr 8: 125.71 – 125.73 Mb
PubMed search	[1]	[2]

Dipeptidase 1 is an enzyme that in humans is encoded by the DPEP1 gene.^[1]

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]^[1]

Interactions

Dipeptidase 1 has been shown to interact with KIAA1279.^[2]

References

1. ^ ^{a b} "Entrez Gene: DPEP1 dipeptidase 1 (renal)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1800. 
2. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 

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. PMC 1136904. PMID 2137335. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1136904. 
• 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. 
• 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. 
• Adachi H, Kubota I, Okamura N, et al. (1989). "Purification and characterization of human microsomal dipeptidase.". J. Biochem. 105 (6): 957–61. PMID 2768222. 
• 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. 
• Satoh S, Ohtsuka K, Keida Y, et al. (1994). "Gene structural analysis and expression of human renal dipeptidase.". Biotechnol. Prog. 10 (2): 134–40. doi:10.1021/bp00026a002. PMID 7764673. 
• 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. 
• 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. 
• 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. 
• 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. doi:10.1016/S0305-0491(99)00039-5. PMID 10425712. 
• 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. doi:10.1016/S0022-2836(02)00632-0. PMID 12144777. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. 
• 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. PMC 2286551. PMID 15340161. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2286551. 
• 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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.