2.3.1.179: beta-ketoacyl-[acyl-carrier-protein] synthase II
This is an abbreviated version!
For detailed information about beta-ketoacyl-[acyl-carrier-protein] synthase II, go to the full flat file.
Word Map on EC 2.3.1.179
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2.3.1.179
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cerulenin
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malonyl-acp
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acyl-acps
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drug development
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cis-vaccenic
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stearoyl-acp
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thiolactomycin
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fasii
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claisen
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biotechnology
- 2.3.1.179
- cerulenin
- malonyl-acp
- acyl-acps
- drug development
-
cis-vaccenic
- stearoyl-acp
- thiolactomycin
- fasii
-
claisen
- biotechnology
Reaction
Synonyms
3-ketoacyl acyl synthase II, 3-ketoacyl-ACP synthase, 3-ketoacyl-ACP synthase 2, 3-ketoacyl-ACP synthase II, 3-oxoacyl-(acylcarrier protein) synthase II, 3-oxoacyl-ACP synthase II, B-ketoacyl-ACP synthase II, beta-ketoacyl ACP-synthase II, beta-ketoacyl acyl carrier protein synthase II, beta-ketoacyl acyl-carrier protein synthase II, beta-ketoacyl synthase II, beta-ketoacyl-(acyl-carrier-protein) synthase II, beta-ketoacyl-ACP synthase FabF3, beta-ketoacyl-ACP synthase II, beta-ketoacyl-acyl carrier protein synthase I/II, beta-ketoacyl-acyl carrier protein synthase II, beta-ketoacyl-acyl carrier protein synthases II, beta-ketoacyl-acyl carrier protein synthetase II, beta-ketoacyl-acyl-carrier protein synthase II, beta-ketoacyl-acyl-carrier-protein synthase II, beta-ketoacyl-[ACP] synthase II, beta-ketoacyl-[ACP] synthase-II, beta-ketoacyl-[acyl carrier protein (ACP)] synthase II, beta-ketoacyl-[acyl-carrier protein (ACP)] synthase II, beta-ketoacyl-[acyl-carrier-protein] synthase II, FabB, FabB/F, FabF, FabF elongation condensing enzyme, FabF of type II fatty acid biosynthesis, FabF1, FASII, fatty acid synthesis type II, KAS II, KAS-II, KAS2, KASII
ECTree
2.3.1.179 beta-ketoacyl-[acyl-carrier-protein] synthase IIAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.3.1.179 - beta-ketoacyl-[acyl-carrier-protein] synthase II
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(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
Acyl carrier protein
0.0017 mM, 50% inhibition of myristic acid transfer from myristoyl-[acyl-carrier protein] to wild-type enzyme
casticin
i.e. 5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-3,6,7-trimethoxy-4H-chromen-4-one
iodoacetamide
prior incubation of the enzymes with fatty acyl thioesters prevents inhibition
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
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
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
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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
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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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
Q7CJ22
inhibitor interaction with the active site, structure analysis, docking study, overview
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