DPEP1

Dipeptidase 1 (renal), also known as DPEP1, is a human gene.cite web | title = Entrez Gene: DPEP1 dipeptidase 1 (renal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1800| accessdate = ]

PBB_Summary
section_title =
summary_text = 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] cite web | title = Entrez Gene: DPEP1 dipeptidase 1 (renal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1800| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hooper NM, Keen JN, Turner AJ |title=Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme. |journal=Biochem. J. |volume=265 |issue= 2 |pages= 429–33 |year= 1990 |pmid= 2137335 |doi=
*cite journal | author=Adachi H, Katayama T, Inuzuka C, "et al." |title=Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form. |journal=J. Biol. Chem. |volume=265 |issue= 25 |pages= 15341–5 |year= 1990 |pmid= 2168407 |doi=
*cite journal | author=Adachi H, Tawaragi Y, Inuzuka C, "et al." |title=Primary structure of human microsomal dipeptidase deduced from molecular cloning. |journal=J. Biol. Chem. |volume=265 |issue= 7 |pages= 3992–5 |year= 1990 |pmid= 2303490 |doi=
*cite journal | author=Adachi H, Kubota I, Okamura N, "et al." |title=Purification and characterization of human microsomal dipeptidase. |journal=J. Biochem. |volume=105 |issue= 6 |pages= 957–61 |year= 1989 |pmid= 2768222 |doi=
*cite journal | author=Austruy E, Jeanpierre C, Antignac C, "et al." |title=Physical and genetic mapping of the dipeptidase gene DPEP1 to 16q24.3. |journal=Genomics |volume=15 |issue= 3 |pages= 684–7 |year= 1993 |pmid= 7682195 |doi= 10.1006/geno.1993.1126
*cite journal | author=Satoh S, Ohtsuka K, Keida Y, "et al." |title=Gene structural analysis and expression of human renal dipeptidase. |journal=Biotechnol. Prog. |volume=10 |issue= 2 |pages= 134–40 |year= 1994 |pmid= 7764673 |doi=
*cite journal | author=Adachi H, Katayama T, Nakazato H, Tsujimoto M |title=Importance of Glu-125 in the catalytic activity of human renal dipeptidase. |journal=Biochim. Biophys. Acta |volume=1163 |issue= 1 |pages= 42–8 |year= 1993 |pmid= 8097406 |doi=
*cite journal | author=Satoh S, Kusunoki C, Konta Y, "et al." |title=Cloning and structural analysis of genomic DNA for human renal dipeptidase. |journal=Biochim. Biophys. Acta |volume=1172 |issue= 1-2 |pages= 181–3 |year= 1993 |pmid= 8439558 |doi=
*cite journal | author=Satoh S, Keida Y, Konta Y, "et al." |title=Purification and molecular cloning of mouse renal dipeptidase. |journal=Biochim. Biophys. Acta |volume=1163 |issue= 3 |pages= 234–42 |year= 1993 |pmid= 8507661 |doi=
*cite journal | author=Kera Y, Liu Z, Matsumoto T, "et al." |title=Rat and human membrane dipeptidase: tissue distribution and developmental changes. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=123 |issue= 1 |pages= 53–8 |year= 1999 |pmid= 10425712 |doi=
*cite journal | author=Nitanai Y, Satow Y, Adachi H, Tsujimoto M |title=Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. |journal=J. Mol. Biol. |volume=321 |issue= 2 |pages= 177–84 |year= 2002 |pmid= 12144777 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=McIver CM, Lloyd JM, Hewett PJ, Hardingham JE |title=Dipeptidase 1: a candidate tumor-specific molecular marker in colorectal carcinoma. |journal=Cancer Lett. |volume=209 |issue= 1 |pages= 67–74 |year= 2004 |pmid= 15145522 |doi= 10.1016/j.canlet.2003.11.033
*cite journal | author=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819–24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209

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