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TargetDipeptidyl peptidase 8
LigandBDBM50506692
Substrate/Competitorn/a
Meas. Tech.ChEMBL_1826908 (CHEMBL4326782)
IC50>100000±n/a nM
Citation Xie, YShao, LWang, QBai, YChen, ZLi, NXu, YLi, YYang, GBian, X Synthesis, nitric oxide release, and dipeptidyl peptidase-4 inhibition of sitagliptin derivatives as new multifunctional antidiabetic agents. Bioorg Med Chem Lett28:3731-3735 (2018) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
Dipeptidyl peptidase 8
Name:Dipeptidyl peptidase 8
Synonyms:DPP8 | DPP8_HUMAN | DPRP-1 | DPRP1 | Dipeptidyl peptidase 8 (DPP-8) | Dipeptidyl peptidase 8 (DPP8) | Dipeptidyl peptidase 8/9 | Dipeptidyl peptidase IV-related protein 1 | Dipeptidyl peptidase VIII | Dipeptidyl peptidase VIII (DDP-VIII) | Prolyl dipeptidase DPP8
Type:Enzyme
Mol. Mass.:103342.62
Organism:Homo sapiens (Human)
Description:Q6V1X1
Residue:898
Sequence:
MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQ
LKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPK
TINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLF
QAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISN
IVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILR
ILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVI
DKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVM
ERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLY
KITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYF
EGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLY
KLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGK
KYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKY
KMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAP
VTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAH
TSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI
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  Blast E-value cutoff:
BDBM50506692
n/a
NameBDBM50506692
Synonyms:CHEMBL4464592
TypeSmall organic molecule
Emp. Form.C21H23F6N5O3
Mol. Mass.507.4294
SMILESOCCCCC(=O)N[C@@H](CC(=O)N1CCn2c(C1)nnc2C(F)(F)F)Cc1cc(F)c(F)cc1F |r|
Structure
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