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(2E)-3-(3-chlorophenyl)-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]prop-2-enamide
ME0619
1,3-dichloro-7-(2,4-dihydroxy-6-methylphenyl)-2,4,6,9-tetrahydroxy-12,12-dimethyltetracen-5(12H)-one
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i.e. fasamycin B
1-chloro-7-(2,4-dihydroxy-6-methylphenyl)-2,4,6,9-tetrahydroxy-12,12-dimethyltetracen-5(12H)-one
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i.e. fasamycin A
2-[(2R)-4-ethyl-3-hydroxy-2-[(1E)-2-methylbuta-1,3-dien-1-yl]-5-oxo-2,5-dihydrothiophen-2-yl]acetamide
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3,6-dichloro-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]-1-benzothiophene-2-carboxamide
ME0640
3,6-dichloro-N-[5-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]pyridin-2-yl]-1-benzothiophene-2-carboxamide
ME0518
3-(benzoylamino)-2-hydroxybenzoic acid
binds outside the active site of the enzyme, binding structure with wild-type and C164Q mutant enzymes, overview. Access to the depths of the active site of the PaFabF apoenzyme is restricted by the conformations of Phe230 and Phe400. 3-(benzoylamino)-2-hydroxybenzoic acid/Mg2+ ion pair selectively binds into and perhaps contributes to the formation of a stable binding site on the surface of the enzyme distant from the active site, from which it is likely to be occluded by steric hindrance
3-benzamido-2-hydroxybenzoic acid
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5-chloro-2-(2,4-dichlorophenoxy)phenol
Acyl carrier protein
0.0017 mM, 50% inhibition of myristic acid transfer from myristoyl-[acyl-carrier protein] to wild-type enzyme
arsenite
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1 mM, 42% inhibition
casticin
i.e. 5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-3,6,7-trimethoxy-4H-chromen-4-one
dihydroplatensimycin
IC50: 97 nM
iodoacetamide
prior incubation of the enzymes with fatty acyl thioesters prevents inhibition
NEM
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5 mM, complete inhibition
PCMB
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1 mM, complete inhibition
5-chloro-2-(2,4-dichlorophenoxy)phenol
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Triclosan
5-chloro-2-(2,4-dichlorophenoxy)phenol
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Triclosan
cerulenin
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0.1 mM, 50% inhibition
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
binding structure with mutant C163Q
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
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0.05 mM, 50% inhibition
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
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blocking active site cysteine
fasamycin A
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fasamycin B
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phomallenic acid C
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platencin
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exhibits a broad-spectrum Gram-positive antibacterial activity through inhibition of fatty acid biosynthesis, targets the two essential proteins, beta-ketoacyl-[acyl carrier protein] synthase II and III, i.e. FabF and FabH, FabF IC50: 113 nM, overview
platencin A1
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also active against FabH, EC 2.3.1.180
platencin A1
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also active against FabH, EC 2.3.1.180
platencin A1
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also active against FabH, EC 2.3.1.180
platensimycin
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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
platensimycin
a natural product inhibitor
platensimycin
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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
platensimycin
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from a strain of Streptomyces platensis MA7339, specifically targets FabF, IC50: 290 nM, exhibits Gram-positive antibacterial activity
thiolactomycin
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thiolactomycin
binding structure with mutant C163Q, IC50: 1.1 mM
Tü3010
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additional information
not inhibited by triclosan
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additional information
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inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition
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additional information
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inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition
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additional information
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in vivo inhibition assays
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additional information
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inhibitors of bacterial FASII can act as potential antibacterial agents, structure-activity relationships of the inhibitors that mainly target beta-ketoacyl-ACP synthase, beta-ketoacyl-ACP reductase, beta-hydroxyacyl-ACP dehydratase, and enoyl-ACP reductase, overview. Screening of phomalenic acids for enzyme inhibition
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additional information
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not inhibited by platensimycin
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additional information
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not inhibited by platensimycin
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additional information
Q7CJ22
inhibitor interaction with the active site, structure analysis, docking study, overview
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