sulbactam [Ligand Id: 10769] activity data from GtoPdb and ChEMBL

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ChEMBL ligand: CHEMBL403 (CP-45899, CP-458992, NSC-759886, Sulbactam)
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  • Beta-lactamase in Pseudomonas aeruginosa [ChEMBL: CHEMBL3885668] [UniProtKB: D2SSQ3]
  • Beta-lactamase in Enterobacter cloacae [ChEMBL: CHEMBL2725] [UniProtKB: P05364]
  • Beta-lactamase in S.aureus [ChEMBL: CHEMBL4114] [UniProtKB: P00807]
  • Beta-lactamase in Bacillus clausii [ChEMBL: CHEMBL5439] [UniProtKB: A8RR46]
  • Beta-lactamase in Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228) [ChEMBL: CHEMBL5031] [UniProtKB: P24735]
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  • Beta-lactamase AmpC in Escherichia coli [ChEMBL: CHEMBL2026] [UniProtKB: P00811]
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  • Beta-lactamase bla(BEL1) in Pseudomonas aeruginosa [ChEMBL: CHEMBL3885670] [UniProtKB: Q3SAW3]
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  • Beta-lactamase OXA-1 in Escherichia coli [ChEMBL: CHEMBL4951] [UniProtKB: P13661]
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  • Beta-lactamase SHV-1 in Escherichia coli [ChEMBL: CHEMBL5956] [UniProtKB: P0AD63]
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  • Beta-lactamase TEM in Escherichia coli [ChEMBL: CHEMBL2065] [UniProtKB: P62593]
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  • Beta-lactamase type II in Bacteroides fragilis [ChEMBL: CHEMBL4840] [UniProtKB: P25910]
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  • Carbapenem-hydrolizing beta-lactamase SFC-1 in Serratia fonticola [ChEMBL: CHEMBL5042] [UniProtKB: Q6JP75]
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  • Extended-spectrum beta-lactamase PER-6 in Aeromonas allosaccharophila [ChEMBL: CHEMBL1697666] [UniProtKB: D5HSX5]
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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]