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Gene and Protein Information | ||||||
Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
Human | - | 863 | 19p13.3 | DPP9 | dipeptidyl peptidase 9 | |
Mouse | - | 862 | 17 D | Dpp9 | dipeptidylpeptidase 9 | |
Rat | - | - | 9q11 | Dpp9 | dipeptidyl peptidase 9 |
Previous and Unofficial Names |
dipeptidyl peptidase IX | DP9 | DPP IX | DPRP2 | dipeptidyl-peptidase 9 |
Database Links | |
Specialist databases | |
MEROPS | S09.019 (Hs) |
Other databases | |
Alphafold | Q86TI2 (Hs), Q8BVG4 (Mm) |
BRENDA | 3.4.14.5 |
CATH/Gene3D | 3.40.50.1820 |
ChEMBL Target | CHEMBL4793 (Hs), CHEMBL3259484 (Mm) |
Ensembl Gene | ENSG00000142002 (Hs), ENSMUSG00000001229 (Mm), ENSRNOG00000050748 (Rn) |
Entrez Gene | 91039 (Hs), 224897 (Mm), 301130 (Rn) |
Human Protein Atlas | ENSG00000142002 (Hs) |
KEGG Enzyme | 3.4.14.5 |
KEGG Gene | hsa:91039 (Hs), mmu:224897 (Mm), rno:301130 (Rn) |
OMIM | 608258 (Hs) |
Orphanet | ORPHA353250 (Hs) |
Pharos | Q86TI2 (Hs) |
RefSeq Nucleotide | NM_139159 (Hs), NM_172624 (Mm) |
RefSeq Protein | NP_631898 (Hs), NP_766212 (Mm) |
UniProtKB | Q86TI2 (Hs), Q8BVG4 (Mm) |
Wikipedia | DPP9 (Hs) |
Enzyme Reaction | ||||
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Substrates and Reaction Kinetics | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Download all structure-activity data for this target as a CSV file
Inhibitors | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Clinically-Relevant Mutations and Pathophysiology | ||||||||||||
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1. Benramdane S, De Loose J, Beyens O, Van Rymenant Y, Vliegen G, Augustyns K, De Winter H, De Meester I, Van der Veken P. (2022) Vildagliptin-Derived Dipeptidyl Peptidase 9 (DPP9) Inhibitors: Identification of a DPP8/9-Specific Lead. ChemMedChem, 17 (15): e202200097. [PMID:35760756]
2. Benramdane S, De Loose J, Filippi N, Espadinha M, Beyens O, Rymenant YV, Dirkx L, Bozdag M, Feijens PB, Augustyns K et al.. (2023) Highly Selective Inhibitors of Dipeptidyl Peptidase 9 (DPP9) Derived from the Clinically Used DPP4-Inhibitor Vildagliptin. J Med Chem, 66 (18): 12717-12738. [PMID:37721854]
3. Connolly BA, Sanford DG, Chiluwal AK, Healey SE, Peters DE, Dimare MT, Wu W, Liu Y, Maw H, Zhou Y et al.. (2008) Dipeptide boronic acid inhibitors of dipeptidyl peptidase IV: determinants of potency and in vivo efficacy and safety. J Med Chem, 51 (19): 6005-13. [PMID:18783201]
4. Fingerlin TE, Murphy E, Zhang W, Peljto AL, Brown KK, Steele MP, Loyd JE, Cosgrove GP, Lynch D, Groshong S et al.. (2013) Genome-wide association study identifies multiple susceptibility loci for pulmonary fibrosis. Nat Genet, 45 (6): 613-20. [PMID:23583980]
5. Meng W, Brigance RP, Chao HJ, Fura A, Harrity T, Marcinkeviciene J, O'Connor SP, Tamura JK, Xie D, Zhang Y et al.. (2010) Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors. J Med Chem, 53 (15): 5620-8. [PMID:20684603]
6. Moore KP, Schwaid AG, Tudor M, Park S, Beshore DC, Converso A, Shipe WD, Anand R, Lan P, Moningka R et al.. (2022) A Phenotypic Screen Identifies Potent DPP9 Inhibitors Capable of Killing HIV-1 Infected Cells. ACS Chem Biol, 17 (9): 2595-2604. [PMID:36044633]
7. Tsai TY, Yeh TK, Chen X, Hsu T, Jao YC, Huang CH, Song JS, Huang YC, Chien CH, Chiu JH et al.. (2010) Substituted 4-carboxymethylpyroglutamic acid diamides as potent and selective inhibitors of fibroblast activation protein. J Med Chem, 53 (18): 6572-83. [PMID:20718420]
8. Van Goethem S, Matheeussen V, Joossens J, Lambeir AM, Chen X, De Meester I, Haemers A, Augustyns K, Van der Veken P. (2011) Structure-activity relationship studies on isoindoline inhibitors of dipeptidyl peptidases 8 and 9 (DPP8, DPP9): is DPP8-selectivity an attainable goal?. J Med Chem, 54 (16): 5737-46. [PMID:21711053]
9. Wu JJ, Tang HK, Yeh TK, Chen CM, Shy HS, Chu YR, Chien CH, Tsai TY, Huang YC, Huang YL et al.. (2009) Biochemistry, pharmacokinetics, and toxicology of a potent and selective DPP8/9 inhibitor. Biochem Pharmacol, 78 (2): 203-10. [PMID:19439267]
10. Yoshida T, Akahoshi F, Sakashita H, Kitajima H, Nakamura M, Sonda S, Takeuchi M, Tanaka Y, Ueda N, Sekiguchi S et al.. (2012) Discovery and preclinical profile of teneligliptin (3-[(2S,4S)-4-[4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl]pyrrolidin-2-ylcarbonyl]thiazolidine): a highly potent, selective, long-lasting and orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes. Bioorg Med Chem, 20 (19): 5705-19. [PMID:22959556]
11. Zhang H, Maqsudi S, Rainczuk A, Duffield N, Lawrence J, Keane FM, Justa-Schuch D, Geiss-Friedlander R, Gorrell MD, Stephens AN. (2015) Identification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis. FEBS J, 282 (19): 3737-57. [PMID:26175140]
S9: Prolyl oligopeptidase: dipeptidyl peptidase 9. Last modified on 10/10/2023. Accessed on 14/09/2024. IUPHAR/BPS Guide to PHARMACOLOGY, https://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2357.