Application | Comment | Organism |
---|---|---|
drug development | fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis and represent increasingly promising targets for the discovery of antibacterial agents with different mechanisms of action | Staphylococcus aureus |
drug development | fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis and represent increasingly promising targets for the discovery of antibacterial agents with different mechanisms of action | Haemophilus influenzae |
drug development | fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis and represent increasingly promising targets for the discovery of antibacterial agents with different mechanisms of action | Enterococcus faecalis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,3-dichloro-7-(2,4-dihydroxy-6-methylphenyl)-2,4,6,9-tetrahydroxy-12,12-dimethyltetracen-5(12H)-one | i.e. fasamycin B | Enterococcus faecalis | |
1-chloro-7-(2,4-dihydroxy-6-methylphenyl)-2,4,6,9-tetrahydroxy-12,12-dimethyltetracen-5(12H)-one | i.e. fasamycin A | Enterococcus faecalis | |
2-[(2R)-4-ethyl-3-hydroxy-2-[(1E)-2-methylbuta-1,3-dien-1-yl]-5-oxo-2,5-dihydrothiophen-2-yl]acetamide | - |
Enterococcus faecalis | |
5-chloro-2-(2,4-dichlorophenoxy)phenol | Triclosan | Haemophilus influenzae | |
5-chloro-2-(2,4-dichlorophenoxy)phenol | Triclosan | Staphylococcus aureus | |
cerulenin | originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF | Enterococcus faecalis | |
cerulenin | originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF | Haemophilus influenzae | |
cerulenin | originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF | Staphylococcus aureus | |
fasamycin A | - |
Staphylococcus aureus | |
fasamycin B | - |
Staphylococcus aureus | |
additional information | 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 | Enterococcus faecalis | |
additional information | 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 | Haemophilus influenzae | |
additional information | 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 | Staphylococcus aureus | |
phomallenic acid C | - |
Haemophilus influenzae | |
phomallenic acid C | - |
Staphylococcus aureus | |
platencin A1 | also active against FabH, EC 2.3.1.180 | Enterococcus faecalis | |
platencin A1 | also active against FabH, EC 2.3.1.180 | Haemophilus influenzae | |
platencin A1 | also active against FabH, EC 2.3.1.180 | Staphylococcus aureus | |
thiolactomycin | - |
Enterococcus faecalis | |
thiolactomycin | - |
Haemophilus influenzae | |
thiolactomycin | - |
Staphylococcus aureus | |
Tü3010 | - |
Haemophilus influenzae | |
Tü3010 | - |
Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Enterococcus faecalis | - |
- |
- |
Haemophilus influenzae | - |
- |
- |
Staphylococcus aureus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] | the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism | Enterococcus faecalis |
Synonyms | Comment | Organism |
---|---|---|
FASII | - |
Staphylococcus aureus |
FASII | - |
Haemophilus influenzae |
FASII | - |
Enterococcus faecalis |
fatty acid synthesis type II | - |
Staphylococcus aureus |
fatty acid synthesis type II | - |
Haemophilus influenzae |
fatty acid synthesis type II | - |
Enterococcus faecalis |
General Information | Comment | Organism |
---|---|---|
physiological function | fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis | Staphylococcus aureus |
physiological function | fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis | Haemophilus influenzae |
physiological function | fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis. All FASII systems have initiation and elongation condensing enzymes which can catalyze the Claisen condensation of an acyl donor and malonyl-ACP to form a beta-ketoacyl-ACP | Enterococcus faecalis |