DPP3

Dipeptidyl-peptidase 3
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsDPP3 ; DPPIII
External IDsOMIM: 606818 MGI: 1922471 HomoloGene: 40210 IUPHAR: 2355 ChEMBL: 4520 GeneCards: DPP3 Gene
EC number3.4.14.4
Orthologs
SpeciesHumanMouse
Entrez1007275221
EnsemblENSG00000254986ENSMUSG00000063904
UniProtQ9NY33Q99KK7
RefSeq (mRNA)NM_001256670NM_133803
RefSeq (protein)NP_001243599NP_598564
Location (UCSC)Chr 11:
66.25 – 66.28 Mb		Chr 19:
4.91 – 4.93 Mb
PubMed search

Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.[1][2]

This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized.[2]

References

  1. ↑ Fukasawa KM, Fukasawa K, Harada M (Jun 2000). "Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12→q13.1 by in situ hybridization". Cytogenet Cell Genet 88 (1–2): 99–100. doi:10.1159/000015498. PMID 10773679.
  2. ↑ 2.0 2.1 "Entrez Gene: DPP3 dipeptidyl-peptidase 3".

Further reading

  • Kar NC, Pearson CM (1978). "Dipeptidyl peptidases in human muscle disease". Clin. Chim. Acta 82 (1–2): 185–92. doi:10.1016/0009-8981(78)90042-6. PMID 618680.
  • Grdisa M, Vitale L (1991). "Types and localization of aminopeptidases in different human blood cells". Int. J. Biochem. 23 (3): 339–45. doi:10.1016/0020-711X(91)90116-5. PMID 2044841.
  • Swanson AA, Davis RM, Meinhardt NC (1985). "Proteases in human lenses and their possible significance". Curr. Eye Res. 4 (1): 43–8. doi:10.3109/02713688508999965. PMID 2858361.
  • Vanha-Perttula T (1989). "Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties". Clin. Chim. Acta 177 (2): 179–95. doi:10.1016/0009-8981(88)90140-4. PMID 2906822.
  • Shimamori Y, Watanabe Y, Fujimoto Y (1989). "Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion". Biochem. Med. Metab. Biol. 40 (3): 305–10. doi:10.1016/0885-4505(88)90133-8. PMID 3233187.
  • Abramić M, Zubanović M, Vitale L (1988). "Dipeptidyl peptidase III from human erythrocytes". Biol. Chem. Hoppe-Seyler 369 (1): 29–38. doi:10.1515/bchm3.1988.369.1.29. PMID 3348886.
  • Shimamori Y, Watanabe Y, Fujimoto Y (1987). "Purification and characterization of dipeptidyl aminopeptidase III from human placenta". Chem. Pharm. Bull. 34 (8): 3333–40. doi:10.1248/cpb.34.3333. PMID 3791505.
  • Swanson AA, Davis RM, McDonald JK (1984). "Dipeptidyl peptidase III of human cataractous lenses. Partial purification". Curr. Eye Res. 3 (2): 287–91. doi:10.3109/02713688408997211. PMID 6368131.
  • Jones TH, Kapralou A (1982). "A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes". Anal. Biochem. 119 (2): 418–23. doi:10.1016/0003-2697(82)90607-8. PMID 7041700.
  • Vitale L, Zubanović M, Abramić M (1982). "Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of human erythrocytes". Acta Biol. Med. Ger. 40 (10–11): 1489–95. PMID 7044004.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Fukasawa K, Fukasawa KM, Kanai M et al. (1998). "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression". Biochem. J. 329 ( Pt 2) (Pt 2): 275–82. PMC 1219041. PMID 9425109.
  • Simaga S, Babić D, Osmak M et al. (1998). "Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue". Eur. J. Cancer 34 (3): 399–405. doi:10.1016/S0959-8049(97)00401-2. PMID 9640230.
  • Akiyama T, Harada S, Kojima F et al. (1998). "Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by Streptomyces sp. TA-3391. I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties". J. Antibiot. 51 (6): 553–9. doi:10.7164/antibiotics.51.553. PMID 9711218.
  • Fukasawa K, Fukasawa KM, Iwamoto H et al. (1999). "The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme". Biochemistry 38 (26): 8299–303. doi:10.1021/bi9904959. PMID 10387075.
  • Hashimoto J, Yamamoto Y, Kurosawa H et al. (2000). "Identification of dipeptidyl peptidase III in human neutrophils". Biochem. Biophys. Res. Commun. 273 (2): 393–7. doi:10.1006/bbrc.2000.2827. PMID 10873616.
  • Abramić M, Schleuder D, Dolovcak L et al. (2001). "Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences". Biol. Chem. 381 (12): 1233–43. doi:10.1515/BC.2000.151. PMID 11209758.
  • 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.

External links