DPEP1

From Wikipedia, the free encyclopedia

Dipeptidase 1 (renal)

PDB rendering based on 1itq.

Available structures: 1itq, 1itu

Identifiers

Symbol(s)

DPEP1; RDP; MBD1; MDP

External IDs

OMIM: 179780 MGI: 94917 HomoloGene: 80192

Gene ontology
Molecular Function:	• membrane dipeptidase activity • metallopeptidase activity • dipeptidyl-peptidase activity • zinc ion binding • metal ion binding • GPI anchor binding
Cellular Component:	• endoplasmic reticulum • microsome • membrane
Biological Process:	• proteolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004413 (mRNA)
NP_004404 (protein)

NM_007876 (mRNA)
NP_031902 (protein)

Location

Chr 16: 88.21 - 88.23 Mb

Chr 8: 126.07 - 126.09 Mb

Pubmed search

[1]

[2]

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

[edit] References

^ ^a ^b Entrez Gene: DPEP1 dipeptidase 1 (renal).

[edit] 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.
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. 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. 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. 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. PMID 12477932.
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. 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.
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.