diphenylamine-2-carboxylic acid [Ligand Id: 4182] activity data from GtoPdb and ChEMBL
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| ChEMBL ligand: CHEMBL23832 (2-Phenylamino-Benzoic Acid, 2-(Phenylamino)Benzoic Acid, Fenamic acid, N-Phenylanthranilic Acid) |
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| DB | Assay description | Assay Type | Standard value | Standard parameter | Original value | Original units | Original parameter | Reference |
|---|---|---|---|---|---|---|---|---|
| Aldo-keto reductase family 1 member C2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5847] [UniProtKB: P52895] | ||||||||
| ChEMBL | Inhibition of AKR1C2 by fluorimetric method | B | 6.36 | pIC50 | 440 | nM | IC50 | Bioorg Med Chem Lett (2011) 21: 1464-1468 [PMID:21277203] |
| ChEMBL | Inhibition of recombinant AKR1C2 assessed as NADP+ dependent oxidation of S-tetralol by fluorescence assay | B | 6.36 | pIC50 | 440 | nM | IC50 | J Med Chem (2012) 55: 2311-2323 [PMID:22263837] |
| ChEMBL | Discontinuous Radiometric Assay: Compounds may be evaluated as selective reversible inhibitors of AKR1C3 by screening them against homogeneous recombinant AKR1C1-AKR1C4 expressed in E. coli. In each case, a discontinuous radiometric assay may be used to monitor the inhibition of progesterone reduction (20-ketosteroid reduction) catalyzed by AKR1C1, the inhibition of Δ4-AD reduction (17-ketosteroid reduction) catalyzed by AKR1C3, and the inhibition of 5α-DHT reduction (3-ketosteroid reduction) catalyzed by AKR1C2 and AKR1C4 (by measuring the formation of 20α-hydroxyprogesterone, testosterone or 3α-androstanediol by radiochromatography). Secondary screens of the compounds of interest include: (a) a full-screen against all nine human recombinant AKR enzymes to ensure there are no-intended off-target effects (in this context AKR1B10 (retinal reductase; SEQ ID NO:5) has been shown to be potently inhibited by N-phenylanthranilates) (Endo et al., 2010, Biol. Pharm. Bull. 33:886-90); (b) a screen against COX-1 and COX-2 to reaffirm that compounds do not act as NSAIDs; and (c) an expanded screen against other nuclear receptors (especially other steroid hormone receptors). | B | 6.36 | pIC50 | 440 | nM | IC50 | US-9271961-B2. Bifunctional AKR1C3 inhibitors/androgen receptor modulators and methods of use thereof (2016) |
| AKR1C3/Aldo-keto-reductase family 1 member C3 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4681] [GtoPdb: 1382] [UniProtKB: P42330] | ||||||||
| ChEMBL | Inhibition of recombinant AKR1C3 assessed as NADP+ dependent oxidation of S-tetralol by fluorescence assay | B | 5.82 | pIC50 | 1520 | nM | IC50 | J Med Chem (2012) 55: 2311-2323 [PMID:22263837] |
| ChEMBL | Inhibition of AKR1C3 by fluorimetric method | B | 5.82 | pIC50 | 1500 | nM | IC50 | Bioorg Med Chem Lett (2011) 21: 1464-1468 [PMID:21277203] |
| ChEMBL | Discontinuous Radiometric Assay: Compounds may be evaluated as selective reversible inhibitors of AKR1C3 by screening them against homogeneous recombinant AKR1C1-AKR1C4 expressed in E. coli. In each case, a discontinuous radiometric assay may be used to monitor the inhibition of progesterone reduction (20-ketosteroid reduction) catalyzed by AKR1C1, the inhibition of Δ4-AD reduction (17-ketosteroid reduction) catalyzed by AKR1C3, and the inhibition of 5α-DHT reduction (3-ketosteroid reduction) catalyzed by AKR1C2 and AKR1C4 (by measuring the formation of 20α-hydroxyprogesterone, testosterone or 3α-androstanediol by radiochromatography). Secondary screens of the compounds of interest include: (a) a full-screen against all nine human recombinant AKR enzymes to ensure there are no-intended off-target effects (in this context AKR1B10 (retinal reductase; SEQ ID NO:5) has been shown to be potently inhibited by N-phenylanthranilates) (Endo et al., 2010, Biol. Pharm. Bull. 33:886-90); (b) a screen against COX-1 and COX-2 to reaffirm that compounds do not act as NSAIDs; and (c) an expanded screen against other nuclear receptors (especially other steroid hormone receptors). | B | 5.82 | pIC50 | 1500 | nM | IC50 | US-9271961-B2. Bifunctional AKR1C3 inhibitors/androgen receptor modulators and methods of use thereof (2016) |
| Carbonic anhydrase 2 in Cryptococcus neoformans var. grubii (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1697676] [UniProtKB: Q3I4V7] | ||||||||
| ChEMBL | Inhibition of Cryptococcus neoformans beta carbonic anhydrase Can2 using CO2 as substrate incubated for 6 hrs prior to substrate addition measured for 10 to 100 secs by stopped flow technique | B | 7.06 | pKi | 87 | nM | Ki | Bioorg Med Chem Lett (2012) 22: 5801-5806 [PMID:22901388] |
| carbonic anhydrase 1/Carbonic anhydrase I in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL261] [GtoPdb: 2597] [UniProtKB: P00915] | ||||||||
| ChEMBL | Inhibition of human CA1 using CO2 as substrate incubated for 6 hrs prior to substrate addition measured for 10 to 100 secs by stopped flow technique | B | 5.92 | pKi | 1200 | nM | Ki | Bioorg Med Chem Lett (2012) 22: 5801-5806 [PMID:22901388] |
| carbonic anhydrase 2/Carbonic anhydrase II in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL205] [GtoPdb: 3092] [UniProtKB: P00918] | ||||||||
| ChEMBL | Inhibition of human CA2 using CO2 as substrate incubated for 6 hrs prior to substrate addition measured for 10 to 100 secs by stopped flow technique | B | 7.42 | pKi | 38 | nM | Ki | Bioorg Med Chem Lett (2012) 22: 5801-5806 [PMID:22901388] |
| carbonic anhydrase 9/Carbonic anhydrase IX in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3594] [GtoPdb: 3055] [UniProtKB: Q16790] | ||||||||
| ChEMBL | Inhibition of human CA9 using CO2 as substrate incubated for 6 hrs prior to substrate addition measured for 10 to 100 secs by stopped flow technique | B | 7.3 | pKi | 50 | nM | Ki | Bioorg Med Chem Lett (2012) 22: 5801-5806 [PMID:22901388] |
| carbonic anhydrase 12/Carbonic anhydrase XII in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3242] [GtoPdb: 2747] [UniProtKB: O43570] | ||||||||
| ChEMBL | Inhibition of human CA12 using CO2 as substrate incubated for 6 hrs prior to substrate addition measured for 10 to 100 secs by stopped flow technique | B | 7.3 | pKi | 50 | nM | Ki | Bioorg Med Chem Lett (2012) 22: 5801-5806 [PMID:22901388] |
| fatty acid binding protein 4/Fatty acid binding protein adipocyte in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2083] [GtoPdb: 2534] [UniProtKB: P15090] | ||||||||
| ChEMBL | Displacement of 1,8-ANS from recombinant human 6His-tagged FABP4 expressed in Escherichia coli BL21 DE3 incubated for 15 mins followed by 1,8-ANS addition and measured after 3 mins by fluorescence based assay | B | 4.3 | pKi | 50690.3 | nM | Ki | J Med Chem (2020) 63: 4090-4106 [PMID:32202425] |
| ChEMBL | Inhibition of FABP4 (unknown origin) | B | 4.29 | pIC50 | 51000 | nM | IC50 | J Med Chem (2022) 65: 84-99 [PMID:34928151] |
| sirtuin 1/NAD-dependent deacetylase sirtuin 1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4506] [GtoPdb: 2707] [UniProtKB: Q96EB6] | ||||||||
| ChEMBL | Inhibition of human recombinant SIRT1 using Fluor de Lys-SIRT as substrate incubated for 60 mins prior to substrate addition measured after 60 mins by fluorimetric analysis | B | 4.17 | pIC50 | 68000 | nM | IC50 | J Med Chem (2012) 55: 5760-5773 [PMID:22642300] |
| ChEMBL | Inhibition of SIRT1 (unknown origin) using acetylated lysine as substrate by Fluor de Lys assay | B | 4.17 | pIC50 | 68000 | nM | IC50 | Eur J Med Chem (2016) 119: 45-69 [PMID:27153347] |
| sirtuin 2/NAD-dependent deacetylase sirtuin 2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4462] [GtoPdb: 2708] [UniProtKB: Q8IXJ6] | ||||||||
| ChEMBL | Inhibition of human recombinant SIRT2 using Fluor de Lys-SIRT as substrate incubated for 60 mins prior to substrate addition measured after 60 mins by fluorimetric analysis | B | 4 | pIC50 | >100000 | nM | IC50 | J Med Chem (2012) 55: 5760-5773 [PMID:22642300] |
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]
