1-methyl-L-tryptophan [Ligand Id: 8225] activity data from GtoPdb and ChEMBL

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ChEMBL ligand: CHEMBL504816 (1-Methyltryptophan)
  • indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase in Human [ChEMBL: CHEMBL4685] [GtoPdb: 2829] [UniProtKB: P14902]
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  • indoleamine 2,3-dioxygenase 1 in Human [GtoPdb: 2829] [UniProtKB: P14902]
  • indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Mouse [ChEMBL: CHEMBL1075294] [GtoPdb: 2829] [UniProtKB: P28776]
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  • indoleamine 2,3-dioxygenase 2/Indoleamine 2,3-dioxygenase 2 in Human [ChEMBL: CHEMBL3627587] [GtoPdb: 3019] [UniProtKB: Q6ZQW0]
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DB Assay description Assay Type Standard value Standard parameter Original value Original units Original parameter Reference
indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4685] [GtoPdb: 2829] [UniProtKB: P14902]
ChEMBL Inhibition of indoleamine 2,3-dioxygenase in aerobic condition B 4.27 pKi 53200 nM Ki Bioorg Med Chem (2008) 16: 8661-8669 [PMID:18715787]
GtoPdb - - 4.37 pKi 42300 nM Ki J Med Chem (2013) 56: 8321-31 [PMID:24099220]
ChEMBL Competitive inhibition of human recombinant IDO1 using L-tryptophan as substrate B 4.37 pKi 42300 nM Ki J Med Chem (2013) 56: 8321-8331 [PMID:24099220]
ChEMBL Inhibition of IDO B 4.43 pKi 37000 nM Ki Bioorg Med Chem (2011) 19: 1550-1561 [PMID:21269836]
ChEMBL Competitive inhibition of IDO1 (unknown origin) using L-tryptophan as substrate incubated for 30 min assessed as reduction in conversion of N-formyl kynurenine to kynurenine by dixon plot analysis B 4.47 pKi 34000 nM Ki WO-2017114260-A1. Uses of tryptanthrin and derivative thereof in preparing hldo2 inhibitor (2017)
ChEMBL Competitive inhibition of human IDO1 in presence of tryptophan B 4.47 pKi 34000 nM Ki J Med Chem (2013) 56: 8321-8331 [PMID:24099220]
ChEMBL Inhibition of IDO1 (unknown origin) B 4.47 pKi 34000 nM Ki Medchemcomm (2019) 10: 1740-1754 [PMID:32055299]
ChEMBL Competitive inhibition of recombinant human IDO1 expressed in Escherichia coli BL21 cells assessed as apparent inhibition constant using varying concentration of L-tryptophan as substrate by Dixon plot analysis B 4.47 pKi 34000 nM Ki J Med Chem (2019) 62: 9161-9174 [PMID:31580660]
ChEMBL Inhibition of IDO1 (unknown origin) B 4.52 pKi 30000 nM Ki Eur J Med Chem (2017) 138: 199-211 [PMID:28667875]
ChEMBL Inhibition of IDO by cell-free assay B 4.72 pKi 19000 nM Ki J Med Chem (2010) 53: 1172-1189 [PMID:20055453]
ChEMBL Competitive inhibition of histidine-tagged human recombinant IDO expressed in bacterial strain BL21 AI using L-Trptophan as substrate measured at 490 nm wavelength after 6 min by colorimetric assay B 5.15 pKi 7000 nM Ki Eur J Med Chem (2011) 46: 3058-3065 [PMID:21419531]
ChEMBL Inhibition of human indoleamine 2,3-dioxygenase expressed in Escherichia coli by spectrophotometric activity assay B 5.18 pKi 6600 nM Ki J Nat Prod (2006) 69: 1496-1499 [PMID:17067170]
ChEMBL Inhibition of recombinant N-terminal His-tagged human IDO (Ala2 to Gly403) overexpressed in Escherichia coli BL21 AI using L-tryptophan as substrate assessed as formation of kynurenine incubated for 5 mins in presence of p-dimethylaminobenzaldehyde B 4 pIC50 100000 nM IC50 Eur J Med Chem (2014) 82: 96-105 [PMID:24878638]
ChEMBL Inhibition of human IDO activity by spectrophotometry B 4 pIC50 100000 nM IC50 Bioorg Med Chem (2011) 19: 1550-1561 [PMID:21269836]
ChEMBL Inhibition of purified recombinant human IDO1 using L-tryptophan substrate incubated fro 30 mins B 4.01 pIC50 98500 nM IC50 Bioorg Med Chem (2019) 27: 3135-3144 [PMID:31178268]
ChEMBL Inhibition of human recombinant IDO expressed in HEK293 cells assessed as blockade of tryptophan degradation by HPLC B 4.05 pIC50 90000 nM IC50 J Med Chem (2010) 53: 1172-1189 [PMID:20055453]
ChEMBL Inhibition of IFNgamma-induced IDO1 in human HeLa cells using L-tryptophan as substrate after 24 hrs B 4.11 pIC50 77290 nM IC50 Eur J Med Chem (2017) 138: 199-211 [PMID:28667875]
ChEMBL Inhibition of recombinant human IDO1 expressed in Escherichia coli BL21(DE3) assessed as effect on kynurenine level using L-tryptophan as substrate incubated for 1 hr by Ehrlich's reagent based assay B 4.38 pIC50 42000 nM IC50 J Med Chem (2020) 63: 15115-15139 [PMID:33215494]
ChEMBL Inhibition of human recombinant IDO1 measured after 60 mins by fluorescence based analysis B 4.38 pIC50 41740 nM IC50 Eur J Med Chem (2023) 254: 115349-115349 [PMID:37060754]
ChEMBL Inhibition of human IDO1 expressed in Escherichia coli BL21 Star assessed as kynurenine formation using L-Trp as substrate preincubated for 90 mins measured after 30 mins by bridge-IT fluorescence assay B 4.46 pIC50 35000 nM IC50 Bioorg Med Chem Lett (2016) 26: 4330-4333 [PMID:27469130]
ChEMBL Inhibition of human IDO1 expressed in HEK293 cells assessed as kynurenine release after 5 hrs by spectrophotometry B 4.74 pIC50 18400 nM IC50 J Med Chem (2013) 56: 8321-8331 [PMID:24099220]
ChEMBL Inhibition of recombinant human IDO1 expressed in HEK293 cells assessed as reduction in kynurenine formation after 5 hrs by microplate reader analysis B 4.74 pIC50 18400 nM IC50 J Med Chem (2019) 62: 9161-9174 [PMID:31580660]
ChEMBL Inhibition of IDO1 in human U87MG cells in presence of L-tryptophan incubated for 24 h B 4.74 pIC50 18400 nM IC50 WO-2017114260-A1. Uses of tryptanthrin and derivative thereof in preparing hldo2 inhibitor (2017)
ChEMBL Inhibition of IDO1 in human HeLa cells B 4.74 pIC50 18400 nM IC50 J Med Chem (2020) 63: 15115-15139 [PMID:33215494]
ChEMBL Inhibition of IDO1 in IFN-gamma treated human HeLa cells incubated for 48 hrs by absorbance based analysis B 4.83 pIC50 14690 nM IC50 Eur J Med Chem (2023) 254: 115349-115349 [PMID:37060754]
ChEMBL Inhibition of His-tagged recombinant human IDO1 expressed in Escherichia coli using tryptophan as substrate by spectrophotometric analysis B 5 pIC50 10000 nM IC50 Bioorg Med Chem (2012) 20: 1354-1363 [PMID:22112538]
ChEMBL Inhibition of N-terminus 6xHis-tagged human IDO1 expressed in Escherichia coli M15 using L-tryptophan as substrate preincubated for 1 hr measured after 15 mins in presence of bovine liver and methylene blue by HPLC analysis B 7.11 pIC50 78 nM IC50 ACS Med Chem Lett (2016) 7: 1167-1172 [PMID:27994758]
indoleamine 2,3-dioxygenase 1 in Human [GtoPdb: 2829] [UniProtKB: P14902]
GtoPdb - - 4.37 pKi 42300 nM Ki J Med Chem (2013) 56: 8321-31 [PMID:24099220]
indoleamine 2,3-dioxygenase 1/Indoleamine 2,3-dioxygenase 1 in Mouse (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1075294] [GtoPdb: 2829] [UniProtKB: P28776]
ChEMBL Inhibition of mouse recombinant IDO expressed in mouse P815B cells assessed as blockade of tryptophan degradation by HPLC B 4.4 pIC50 40000 nM IC50 J Med Chem (2010) 53: 1172-1189 [PMID:20055453]
indoleamine 2,3-dioxygenase 2/Indoleamine 2,3-dioxygenase 2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3627587] [GtoPdb: 3019] [UniProtKB: Q6ZQW0]
ChEMBL Inhibition of IDO2 (unknown origin) expressed in human U87MG cells in presence of L-tryptophan incubated for 24 h B 4.08 pIC50 82530 nM IC50 WO-2017114260-A1. Uses of tryptanthrin and derivative thereof in preparing hldo2 inhibitor (2017)
ChEMBL Inhibition of recombinant human C-terminal His6-tagged IDO2 (14-420 residues) expressed in Escherichia coli BL21(DE3) assessed as reduction in L-kynurenine formation using L-tryptophan as substrate after 30 mins in presence of catalase by methylene blue dye based assay B 4.08 pIC50 82500 nM IC50 Eur J Med Chem (2016) 123: 171-179 [PMID:27475108]
ChEMBL Inhibition of human IDO2 using L-tryptophan as substrate assessed as reduction in conversion of N-formyl kynurenine to kynurenine B 4.24 pIC50 56960 nM IC50 WO-2017114260-A1. Uses of tryptanthrin and derivative thereof in preparing hldo2 inhibitor (2017)
ChEMBL Inhibition of recombinant human IDO2 expressed in human U87MG cells assessed as reduction in kynurenine formation using L-tryptophan as substrate after 6 hrs by spectrophotometry B 4.24 pIC50 56900 nM IC50 Eur J Med Chem (2016) 123: 171-179 [PMID:27475108]
ChEMBL Inhibition of human IDO2 expressed in Escherichia coli BL21 Star assessed as kynurenine formation using L-Trp as substrate preincubated for 90 mins measured after 30 mins by bridge-IT fluorescence assay B 4.46 pIC50 35000 nM IC50 Bioorg Med Chem Lett (2016) 26: 4330-4333 [PMID:27469130]

ChEMBL data shown on this page come from version 34:

Zdrazil B, Felix E, Hunter F, Manners EJ, Blackshaw J, Corbett S, de Veij M, Ioannidis H, Lopez DM, Mosquera JF, Magarinos MP, Bosc N, Arcila R, Kizilören T, Gaulton A, Bento AP, Adasme MF, Monecke P, Landrum GA, Leach AR. (2024). The ChEMBL Database in 2023: a drug discovery platform spanning multiple bioactivity data types and time periods. Nucleic Acids Res., 52(D1). DOI: 10.1093/nar/gkad1004. [EPMCID:10767899] [PMID:37933841]
Davies M, Nowotka M, Papadatos G, Dedman N, Gaulton A, Atkinson F, Bellis L, Overington JP. (2015) 'ChEMBL web services: streamlining access to drug discovery data and utilities.' Nucleic Acids Res., 43(W1). DOI: 10.1093/nar/gkv352. [EPMCID:25883136]