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Literature summary for 2.3.1.179 extracted from

  • Wang, J.; Soisson, S.M.; Young, K.; Shoop, W.; Kodali, S.; Galgoci, A.; Painter, R.; Parthasarathy, G.; Tang, Y.S.; Cummings, R.; Ha, S.; Dorso, K.; Motyl, M.; Jayasuriya, H.; Ondeyka, J.; Herath, K.; Zhang, C.; Hernandez, L.; Allocco, J.; Basilio, A.; Tormo, J.R.; Genilloud, O.; Vicente, F.; Pelaez, F.
    Platensimycin is a selective FabF inhibitor with potent antibiotic properties (2006), Nature, 441, 358-361.
    View publication on PubMed
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Application

Application Comment Organism
drug development the enzyme is a target for antibacterial drugs Staphylococcus aureus
drug development the enzyme is a target for antibacterial drugs Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure determination and analysis at 2.6 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
C163Q site-directed mutagenesis, interaction with platensimycin compared to the interaction with the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
cerulenin binding structure with mutant C163Q Escherichia coli
dihydroplatensimycin IC50: 97 nM Escherichia coli
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
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
thiolactomycin binding structure with mutant C163Q, IC50: 1.1 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AAI5
-
-
Staphylococcus aureus
-
-
-

Synonyms

Synonyms Comment Organism
FabF
-
 Staphylococcus aureus
FabF
-
 Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
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
0.000097
-
 IC50: 97 nM Escherichia coli dihydroplatensimycin
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
1.1
-
 binding structure with mutant C163Q, IC50: 1.1 mM Escherichia coli thiolactomycin