EC Number | Application | Comment | Organism |
---|---|---|---|
2.3.1.179 | drug development | the enzyme is a target for antibacterial drugs | Staphylococcus aureus |
2.3.1.179 | drug development | the enzyme is a target for antibacterial drugs | Escherichia coli |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.3.1.179 | crystal structure determination and analysis at 2.6 A resolution | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.179 | C163Q | site-directed mutagenesis, interaction with platensimycin compared to the interaction with the wild-type enzyme | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.179 | cerulenin | binding structure with mutant C163Q | Escherichia coli | |
2.3.1.179 | dihydroplatensimycin | IC50: 97 nM | Escherichia coli | |
2.3.1.179 | platensimycin | from Streptomyces platensis, IC50: 160 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with the acyl-enzyme intermediate of the target protein, a specific conformational change that occurs on acylation must take place before the inhibitor can bind, overview, platensimycin shows no cross-resistance to other key antibiotic-resistant strains, binding structure with mutant C163Q | Escherichia coli | |
2.3.1.179 | platensimycin | from Streptomyces platensis, IC50: 48 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with the acyl-enzyme intermediate of the target protein, a specific conformational change that occurs on acylation must take place before the inhibitor can bind, overview, platensimycin shows no cross-resistance to other key antibiotic-resistant strains | Staphylococcus aureus | |
2.3.1.179 | thiolactomycin | binding structure with mutant C163Q, IC50: 1.1 mM | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.179 | Escherichia coli | P0AAI5 | - |
- |
2.3.1.179 | Staphylococcus aureus | - |
- |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.179 | FabF | - |
Staphylococcus aureus |
2.3.1.179 | FabF | - |
Escherichia coli |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.3.1.179 | 0.000048 | - |
from Streptomyces platensis, IC50: 48 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with th | Staphylococcus aureus | platensimycin | |
2.3.1.179 | 0.000097 | - |
IC50: 97 nM | Escherichia coli | dihydroplatensimycin | |
2.3.1.179 | 0.00016 | - |
from Streptomyces platensis, IC50: 160 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with t | Escherichia coli | platensimycin | |
2.3.1.179 | 1.1 | - |
binding structure with mutant C163Q, IC50: 1.1 mM | Escherichia coli | thiolactomycin |