Dipeptidase 1

DPEP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ITQ, 1ITU
Identifiers
Aliases	DPEP1, MBD1, MDP, RDP, dipeptidase 1 (renal)
External IDs	MGI: 94917 HomoloGene: 80192 GeneCards: DPEP1
Gene ontology Molecular function • metallodipeptidase activity • zinc ion binding • metal ion binding • cysteine-type endopeptidase inhibitor activity involved in apoptotic process • peptidase activity • GPI anchor binding • modified amino acid binding • protein binding • metalloexopeptidase activity • hydrolase activity • metallopeptidase activity • dipeptidyl-peptidase activity • dipeptidase activity Cellular component • cell projection • membrane • plasma membrane • apical part of cell • extracellular space • apical plasma membrane • anchored component of membrane • extracellular exosome • microvillus membrane Biological process • cellular response to calcium ion • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process • leukotriene metabolic process • glutathione metabolic process • antibiotic metabolic process • negative regulation of apoptotic process • proteolysis • cellular response to drug • negative regulation of cell migration • xenobiotic metabolic process • cellular response to nitric oxide • homocysteine metabolic process • cellular lactam catabolic process • apoptotic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1800	13479
Ensembl	ENSG00000015413	ENSMUSG00000019278
UniProt	P16444	P31428
RefSeq (mRNA)	NM_001128141 NM_004413	NM_007876
RefSeq (protein)	NP_001121613.1 NP_004404.1	NP_031902.2
Location (UCSC)	Chr 16: 89.61 – 89.64 Mb	Chr 8: 123.19 – 123.2 Mb
PubMed search	[1]	[2]
Wikidata

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Dipeptidase 1 is an enzyme that in humans is encoded by the DPEP1 gene.^[3]

Function

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]^[3]

Interactions

Dipeptidase 1 has been shown to interact with KIAA1279.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: DPEP1 dipeptidase 1 (renal)".
4. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

Further reading

• Hooper NM, Keen JN, Turner AJ (Jan 1990). "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme". The Biochemical Journal. 265 (2): 429–33. PMC 1136904. PMID 2137335.
• Adachi H, Katayama T, Inuzuka C, Oikawa S, Tsujimoto M, Nakazato H (Sep 1990). "Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form". The Journal of Biological Chemistry. 265 (25): 15341–5. PMID 2168407.
• Adachi H, Tawaragi Y, Inuzuka C, Kubota I, Tsujimoto M, Nishihara T, Nakazato H (Mar 1990). "Primary structure of human microsomal dipeptidase deduced from molecular cloning". The Journal of Biological Chemistry. 265 (7): 3992–5. PMID 2303490.
• Adachi H, Kubota I, Okamura N, Iwata H, Tsujimoto M, Nakazato H, Nishihara T, Noguchi T (Jun 1989). "Purification and characterization of human microsomal dipeptidase". Journal of Biochemistry. 105 (6): 957–61. PMID 2768222.
• Austruy E, Jeanpierre C, Antignac C, Whitmore SA, Van Cong N, Bernheim A, Callen DF, Junien C (Mar 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, Kusunoki C, Konta Y, Niwa M, Kohsaka M (1994). "Gene structural analysis and expression of human renal dipeptidase". Biotechnology Progress. 10 (2): 134–40. doi:10.1021/bp00026a002. PMID 7764673.
• Adachi H, Katayama T, Nakazato H, Tsujimoto M (Apr 1993). "Importance of Glu-125 in the catalytic activity of human renal dipeptidase". Biochimica et Biophysica Acta. 1163 (1): 42–8. doi:10.1016/0167-4838(93)90276-w. PMID 8097406.
• Satoh S, Kusunoki C, Konta Y, Niwa M, Kohsaka M (Feb 1993). "Cloning and structural analysis of genomic DNA for human renal dipeptidase". Biochimica et Biophysica Acta. 1172 (1-2): 181–3. doi:10.1016/0167-4781(93)90289-p. PMID 8439558.
• Satoh S, Keida Y, Konta Y, Maeda M, Matsumoto Y, Niwa M, Kohsaka M (Jun 1993). "Purification and molecular cloning of mouse renal dipeptidase". Biochimica et Biophysica Acta. 1163 (3): 234–42. doi:10.1016/0167-4838(93)90157-m. PMID 8507661.
• Kera Y, Liu Z, Matsumoto T, Sorimachi Y, Nagasaki H, Yamada RH (May 1999). "Rat and human membrane dipeptidase: tissue distribution and developmental changes". Comparative Biochemistry and Physiology B. 123 (1): 53–8. doi:10.1016/S0305-0491(99)00039-5. PMID 10425712.
• Nitanai Y, Satow Y, Adachi H, Tsujimoto M (Aug 2002). "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis". Journal of Molecular Biology. 321 (2): 177–84. doi:10.1016/S0022-2836(02)00632-0. PMID 12144777.
• McIver CM, Lloyd JM, Hewett PJ, Hardingham JE (Jun 2004). "Dipeptidase 1: a candidate tumor-specific molecular marker in colorectal carcinoma". Cancer Letters. 209 (1): 67–74. doi:10.1016/j.canlet.2003.11.033. PMID 15145522.
• Zhang Z, Henzel WJ (Oct 2004). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Science. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMC 2286551. PMID 15340161.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.