Click here for a description of the charts and data table
Please tell us if you are using this feature and what you think!
ChEMBL ligand: CHEMBL403 (CP-45899, CP-458992, NSC-759886, Sulbactam) |
---|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
There should be some charts here, you may need to enable JavaScript!
|
DB | Assay description | Assay Type | Standard value | Standard parameter | Original value | Original units | Original parameter | Reference |
---|---|---|---|---|---|---|---|---|
ADC-14 protein in Acinetobacter genomosp. 3 (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1667675] [UniProtKB: Q0VTR6] | ||||||||
ChEMBL | Inhibition of Acinetobacter genomosp. 3 isolate 65 ADC-14 | B | 5.95 | pIC50 | 1120 | nM | IC50 | Antimicrob Agents Chemother (2009) 53: 1177-1184 [PMID:19029333] |
ADC-16 protein in Acinetobacter genomosp. 3 (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1667676] [UniProtKB: Q0VTR8] | ||||||||
ChEMBL | Inhibition of Acinetobacter genomosp. 3 isolate 103 ADC-16 | B | 5.11 | pIC50 | 7758 | nM | IC50 | Antimicrob Agents Chemother (2009) 53: 1177-1184 [PMID:19029333] |
ADC-18 protein in Acinetobacter genomosp. 3 (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1667677] [UniProtKB: Q0VTS0] | ||||||||
ChEMBL | Inhibition of Acinetobacter genomosp. 3 isolate 195 ADC-18 | B | 4.93 | pIC50 | 11650 | nM | IC50 | Antimicrob Agents Chemother (2009) 53: 1177-1184 [PMID:19029333] |
Bacterial beta-lactamase TEM in Bacteria (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2364670] [UniProtKB: P62593] | ||||||||
ChEMBL | Cell Free Inhibition Assay: The inhibitory concentrations (IC50, [uM]) of the beta -lactamase inhibitors against purified TEM-1, SHV-1 and AmpC beta -lactamases are assessed by determining the concentration of inhibitor at which 50% of the nitrocefin hydrolysis is inhibited by the particular enzyme. Assays are performed with beta -lactamases expressed in the pET system (Novagen, San Diego, Calif.) without signal peptides. They contain an N-terminal hexa-Histidine tag that is used for purification on Ni-NTA (Qiagen, Hilden, Germany). The compounds are prepared as 50 mM stocks in DMSO and diluted into buffer P1 (50 mM phosphate, pH 7) to a final concentration of 10% DMSO. All further dilutions are done in P2 (P1 with 10% DMSO). Enzyme and compound dilutions are pre-incubated for 10 min at 37 C. and the reaction is started with the addition of pre-warmed (37 C.) nitrocefin at a final concentration of 50 mM. The change in absorption at 490 nm is followed at 37 C. for 10 min with 30 s intervals. | B | 5.97 | pIC50 | 1065.9 | nM | IC50 | US-9120808-B2. Substituted clavulanic acid (2015) |
Beta-lactamase in Pseudomonas aeruginosa (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3885668] [UniProtKB: D2SSQ3] | ||||||||
ChEMBL | Inhibition of Pseudomonas aeruginosa 531 beta-lactamase BEL-2 | B | 5.52 | pIC50 | 3000 | nM | IC50 | Antimicrob Agents Chemother (2010) 54: 533-535 [PMID:19884378] |
Beta-lactamase in Enterobacter cloacae (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2725] [UniProtKB: P05364] | ||||||||
ChEMBL | In vitro inhibitory activity against Beta-lactamase AmpC of class C enzyme | B | 4.18 | pIC50 | 66000 | nM | IC50 | J Med Chem (2003) 46: 2569-2571 [PMID:12801220] |
ChEMBL | Inhibition of Enterobacter cloacae beta-lactamase P99 assessed as nitrocefin hydrolysis after 5 mins enzyme-compound preincubation | B | 4.68 | pIC50 | 21100 | nM | IC50 | Antimicrob Agents Chemother (2010) 54: 5132-5138 [PMID:20921316] |
ChEMBL | In vitro inhibitory activity against Beta-lactamase TEM-1 of class A enzyme | B | 5.85 | pIC50 | 1400 | nM | IC50 | J Med Chem (2003) 46: 2569-2571 [PMID:12801220] |
ChEMBL | Compound was evaluated for beta-lactamase inhibition activity of Escherichia cloacae after 15 min of pre-incubation with the enzyme at 37 degree C | B | 6 | pIC50 | 1000 | nM | IC50 | Bioorg Med Chem Lett (1997) 7: 2217-2222 |
Beta-lactamase in S.aureus (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4114] [UniProtKB: P00807] | ||||||||
ChEMBL | Inhibitory activity against Penicillinase from Staphylococcus aureus TH-14 using piperacillin (40 uM) as a substrate | B | 5.19 | pIC50 | 6500 | nM | IC50 | J Med Chem (1987) 30: 1469-1474 [PMID:3039137] |
Beta-lactamase in Bacillus clausii (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5439] [UniProtKB: A8RR46] | ||||||||
ChEMBL | Inhibition of Bacillus clausii NR beta-lactamase BCL1 expressed in Escherichia coli BL21 (DE3) | B | 7.12 | pIC50 | 75 | nM | IC50 | Antimicrob Agents Chemother (2007) 51: 4009-4014 [PMID:17846134] |
Beta-lactamase in Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228) (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5031] [UniProtKB: P24735] | ||||||||
ChEMBL | Inhibition of Pseudomonas aeruginosa beta-lactamase AmpC assessed as nitrocefin hydrolysis after 5 mins enzyme-compound preincubation | B | 4.57 | pIC50 | 27000 | nM | IC50 | Antimicrob Agents Chemother (2010) 54: 5132-5138 [PMID:20921316] |
Beta-lactamase 1 in Bacillus cereus (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5732] [UniProtKB: P00809] | ||||||||
ChEMBL | Inhibition of Beta-lactamase of Bacillus cereus (class A enzyme) without pre-incubation | B | 4.6 | pIC50 | 25000 | nM | IC50 | Bioorg Med Chem Lett (1995) 5: 2037-2040 |
ChEMBL | Tested for the ability to inhibit Beta-lactamase of Bacillus cereus (class A enzyme) with 10 minutes pre-incubation | B | 4.6 | pIC50 | 25000 | nM | IC50 | Bioorg Med Chem Lett (1995) 5: 2037-2040 |
Beta-lactamase AmpC in Escherichia coli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2026] [UniProtKB: P00811] | ||||||||
ChEMBL | In vitro inhibitory concentration against AmpC enzyme | B | 4.18 | pIC50 | 66000 | nM | IC50 | Bioorg Med Chem Lett (2001) 11: 997-1000 [PMID:11327608] |
ChEMBL | Inhibitory activity against AmpC (class C) beta-lactamase | B | 4.18 | pIC50 | 65900 | nM | IC50 | Bioorg Med Chem Lett (1999) 9: 991-996 [PMID:10230626] |
ChEMBL | Inhibitory activity against AmpC (class C) beta-lactamase | B | 4.18 | pIC50 | 65900 | nM | IC50 | Bioorg Med Chem Lett (1999) 9: 997-1002 [PMID:10230627] |
ChEMBL | Cell Free Inhibition Assay: The inhibitory concentrations (IC50, [uM]) of the beta -lactamase inhibitors against purified TEM-1, SHV-1 and AmpC beta -lactamases are assessed by determining the concentration of inhibitor at which 50% of the nitrocefin hydrolysis is inhibited by the particular enzyme. Assays are performed with beta -lactamases expressed in the pET system (Novagen, San Diego, Calif.) without signal peptides. They contain an N-terminal hexa-Histidine tag that is used for purification on Ni-NTA (Qiagen, Hilden, Germany). The compounds are prepared as 50 mM stocks in DMSO and diluted into buffer P1 (50 mM phosphate, pH 7) to a final concentration of 10% DMSO. All further dilutions are done in P2 (P1 with 10% DMSO). Enzyme and compound dilutions are pre-incubated for 10 min at 37 C. and the reaction is started with the addition of pre-warmed (37 C.) nitrocefin at a final concentration of 50 mM. The change in absorption at 490 nm is followed at 37 C. for 10 min with 30 s intervals. | B | 4.59 | pIC50 | 25495.4 | nM | IC50 | US-9120808-B2. Substituted clavulanic acid (2015) |
Beta-lactamase bla(BEL1) in Pseudomonas aeruginosa (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3885670] [UniProtKB: Q3SAW3] | ||||||||
ChEMBL | Inhibition of Pseudomonas aeruginosa 51170 beta-lactamase BEL-1 | B | 5.52 | pIC50 | 3000 | nM | IC50 | Antimicrob Agents Chemother (2010) 54: 533-535 [PMID:19884378] |
Beta-lactamase GES-13 in Pseudomonas aeruginosa (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1250341] [UniProtKB: D1MIX9] | ||||||||
ChEMBL | Inhibition of Pseudomonas aeruginosa GES-13 beta lactamase | B | 6.43 | pIC50 | 370 | nM | IC50 | Antimicrob Agents Chemother (2010) 54: 1331-1333 [PMID:20065056] |
Beta-lactamase OXA-1 in Escherichia coli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4951] [UniProtKB: P13661] | ||||||||
ChEMBL | Inhibitory activity against Beta-lactamase type OXA1 (penicillinase) from Escherichia coli OXA1 using ampicillin (40 uM) as a substrate | B | 4.66 | pIC50 | 22000 | nM | IC50 | J Med Chem (1987) 30: 1469-1474 [PMID:3039137] |
Beta-lactamase SCO-1 in Escherichia coli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1075073] [UniProtKB: A1E3K9] | ||||||||
ChEMBL | Inhibition of Escherichia coli beta-lactamase SCO1 | B | 5.21 | pIC50 | 6200 | nM | IC50 | Antimicrob Agents Chemother (2007) 51: 2185-2188 [PMID:17353248] |
Beta-lactamase SHV-1 in Escherichia coli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5956] [UniProtKB: P0AD63] | ||||||||
ChEMBL | Cell Free Inhibition Assay: The inhibitory concentrations (IC50, [uM]) of the beta -lactamase inhibitors against purified TEM-1, SHV-1 and AmpC beta -lactamases are assessed by determining the concentration of inhibitor at which 50% of the nitrocefin hydrolysis is inhibited by the particular enzyme. Assays are performed with beta -lactamases expressed in the pET system (Novagen, San Diego, Calif.) without signal peptides. They contain an N-terminal hexa-Histidine tag that is used for purification on Ni-NTA (Qiagen, Hilden, Germany). The compounds are prepared as 50 mM stocks in DMSO and diluted into buffer P1 (50 mM phosphate, pH 7) to a final concentration of 10% DMSO. All further dilutions are done in P2 (P1 with 10% DMSO). Enzyme and compound dilutions are pre-incubated for 10 min at 37 C. and the reaction is started with the addition of pre-warmed (37 C.) nitrocefin at a final concentration of 50 mM. The change in absorption at 490 nm is followed at 37 C. for 10 min with 30 s intervals. | B | 5.41 | pIC50 | 3915 | nM | IC50 | US-9120808-B2. Substituted clavulanic acid (2015) |
Beta-lactamase SHV-11 in Escherichia coli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1287606] [UniProtKB: Q7X575] | ||||||||
ChEMBL | Inhibition of Escherichia coli JM109 beta-lactamase SHV-11 | B | 5.62 | pIC50 | 2400 | nM | IC50 | Antimicrob Agents Chemother (2008) 52: 3792-3794 [PMID:18663019] |
Beta-lactamase TEM in Escherichia coli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL2065] [UniProtKB: P62593] | ||||||||
ChEMBL | Inhibition constant (Ki) for TEM-1 beta-lactamase | B | 6.1 | pKi | 800 | nM | Ki | J Med Chem (1988) 31: 370-374 [PMID:3257523] |
ChEMBL | Inhibitory activity against Beta-lactamase from Bacillus sp. using penicillin G as substrate | B | 5 | pIC50 | 10000 | nM | IC50 | J Med Chem (1987) 30: 1469-1474 [PMID:3039137] |
ChEMBL | Inhibition of Escherichia coli K12 TEM1 | B | 5.14 | pIC50 | 7300 | nM | IC50 | Antimicrob Agents Chemother (2007) 51: 2185-2188 [PMID:17353248] |
ChEMBL | Inhibitory activity against TEM-1 (class A) beta-lactamase | B | 5.85 | pIC50 | 1400 | nM | IC50 | Bioorg Med Chem Lett (1999) 9: 991-996 [PMID:10230626] |
ChEMBL | Inhibitory activity against TEM-1 (class A) beta-lactamase | B | 5.85 | pIC50 | 1400 | nM | IC50 | Bioorg Med Chem Lett (1999) 9: 997-1002 [PMID:10230627] |
ChEMBL | In vitro inhibitory concentration against TEM-1 enzyme | B | 5.85 | pIC50 | 1400 | nM | IC50 | Bioorg Med Chem Lett (2001) 11: 997-1000 [PMID:11327608] |
ChEMBL | Compound was evaluated for beta-lactamase inhibition activity of Escherichia coli after 15 min of pre-incubation with the enzyme at 37 degree C | B | 6.1 | pIC50 | 800 | nM | IC50 | Bioorg Med Chem Lett (1997) 7: 2217-2222 |
Beta-lactamase type II in Bacteroides fragilis (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4840] [UniProtKB: P25910] | ||||||||
ChEMBL | In vitro inhibitory concentration against CCRA enzyme | B | 4 | pIC50 | >100000 | nM | IC50 | Bioorg Med Chem Lett (2001) 11: 997-1000 [PMID:11327608] |
Carbapenem-hydrolizing beta-lactamase SFC-1 in Serratia fonticola (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL5042] [UniProtKB: Q6JP75] | ||||||||
ChEMBL | Inhibition of Serratia fonticola UTAD54 SFC1 beta lactamase expressed in Escherichia coli BL21(DE3) by SDS-PAGE | B | 4.64 | pIC50 | 22700 | nM | IC50 | Antimicrob Agents Chemother (2007) 51: 4512-4514 [PMID:17875998] |
Class D beta-lactamase in Brachyspira pilosicoli (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1255145] [UniProtKB: Q50H31] | ||||||||
ChEMBL | Inhibition of Brachyspira pilosicoli beta-lactamase OXA-63 expressed in Escherichia coli BL21 (DE3) assessed as reduction in nitrocefin hydrolysis by spectrophotometry relative to oxacillin | B | 4.92 | pIC50 | 12000 | nM | IC50 | Antimicrob Agents Chemother (2008) 52: 1264-1268 [PMID:18212108] |
Extended-spectrum beta-lactamase PER-6 in Aeromonas allosaccharophila (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1697666] [UniProtKB: D5HSX5] | ||||||||
ChEMBL | Inhibition of Aeromonas allosaccharophila AL-1 beta-lactamase PER6 | B | 5.4 | pIC50 | 4000 | nM | IC50 | Antimicrob Agents Chemother (2010) 54: 1619-1622 [PMID:20145085] |
ChEMBL data shown on this page come from version 33:
Mendez D, Gaulton A, Bento AP, Chambers J, De Veij M, Félix E, Magariños MP, Mosquera JF, Mutowo P, Nowotka M, Gordillo-Marañón M, Hunter F, Junco L, Mugumbate G, Rodriguez-Lopez M, Atkinson F, Bosc N, Radoux CJ, Segura-Cabrera A, Hersey A, Leach AR. (2019) 'ChEMBL: towards direct deposition of bioassay data' Nucleic Acids Res., 47(D1). DOI: 10.1093/nar/gky1075. [EPMCID:30398643]
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]