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Literature summary extracted from

  • Wang, Y.; Ma, S.
    Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents (2013), ChemMedChem, 8, 1589-1608.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.1.179 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
2.3.1.179 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
2.3.1.179 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

EC Number Inhibitors Comment Organism Structure
2.3.1.179 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
2.3.1.179 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
2.3.1.179 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
2.3.1.179 5-chloro-2-(2,4-dichlorophenoxy)phenol Triclosan Haemophilus influenzae
2.3.1.179 5-chloro-2-(2,4-dichlorophenoxy)phenol Triclosan Staphylococcus aureus
2.3.1.179 cerulenin originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF Enterococcus faecalis
2.3.1.179 cerulenin originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF Haemophilus influenzae
2.3.1.179 cerulenin originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF Staphylococcus aureus
2.3.1.179 fasamycin A
-
 Staphylococcus aureus
2.3.1.179 fasamycin B
-
 Staphylococcus aureus
2.3.1.179 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
2.3.1.179 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
2.3.1.179 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
2.3.1.179 phomallenic acid C
-
 Haemophilus influenzae
2.3.1.179 phomallenic acid C
-
 Staphylococcus aureus
2.3.1.179 platencin A1 also active against FabH, EC 2.3.1.180 Enterococcus faecalis
2.3.1.179 platencin A1 also active against FabH, EC 2.3.1.180 Haemophilus influenzae
2.3.1.179 platencin A1 also active against FabH, EC 2.3.1.180 Staphylococcus aureus
2.3.1.179 thiolactomycin
-
 Enterococcus faecalis
2.3.1.179 thiolactomycin
-
 Haemophilus influenzae
2.3.1.179 thiolactomycin
-
 Staphylococcus aureus
2.3.1.179 Tü3010
-
 Haemophilus influenzae
2.3.1.179 Tü3010
-
 Staphylococcus aureus
2.3.1.180 1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl (2E)-3-(biphenyl-4-yl)prop-2-enoate
-
 Escherichia coli
2.3.1.180 1-(4-[(E)-[3-(benzyloxy)benzylidene]amino]phenyl)-3-phenylthiourea molecular docking indicates that the compound has one hydrogen bonding interaction with Thr 81 of Escherichia coli FabH Escherichia coli
2.3.1.180 1-(5-bromo-2-hydroxybenzyl)-1-(4-chlorophenyl)-3-phenylurea
-
 Escherichia coli
2.3.1.180 1-(5-carboxypentyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
-
 Escherichia coli
2.3.1.180 1-cyclohexyl-N-(2'-hydroxy-1,1':3',1''-terphenyl-5'-yl)-5-oxopyrrolidine-3-carboxamide
-
 Escherichia coli
2.3.1.180 1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
 Escherichia coli
2.3.1.180 2,4-dibromo-6-[(E)-[2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]phenol the binding model demonstrated that the phenolic hydroxy group of 40 interacts with the amino hydrogen of Asn247 of Escherichia coli FabH by hydrogen bonds Escherichia coli
2.3.1.180 2-(2-methoxyphenyl)-5-[(2-methyl-5-nitro-1H-imidazol-1-yl)methyl]-1,3,4-oxadiazole
-
 Escherichia coli
2.3.1.180 2-[3-(3,4-dichlorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
 Escherichia coli
2.3.1.180 2-[4-(2,4-dinitrophenyl)-1H-pyrazol-1-yl]-4-(trifluoromethyl)pyrimidine
-
 Escherichia coli
2.3.1.180 4,5-dichloro-3H-1,2-dithiol-3-one
-
 Escherichia coli
2.3.1.180 4-fluoro-2-[(E)-[[2-(4-hydroxyphenyl)ethyl]imino]methyl]phenol
-
 Escherichia coli
2.3.1.180 4-[(1Z)-N,2-bis(4-chlorophenyl)ethanimidoyl]benzene-1,3-diol
-
 Escherichia coli
2.3.1.180 5-ethyl-4-fluoro-2-[(2-fluoropyridin-3-yl)oxy]phenol
-
 Escherichia coli
2.3.1.180 5-hydroxy-2-phenyl-7-[3-(pyrrolidin-1-yl)propoxy]-2,3-dihydro-4H-chromen-4-one a strong inhibitor, interacts with Escherichia coli FabH via a hydrogen bond between its 5-hydroxy group and the amino hydrogen of Asn247 and a hydrophobic interaction between the pyrrolidine moiety at the C7 position and Asn274, Ile 156, Phe157, and Met2 Escherichia coli
2.3.1.180 5-[(2,6-dichlorobenzyl)oxy]-1-[(6-methyl-1,3-benzodioxol-5-yl)methyl]-1H-indole-2-carboxylic acid
-
 Escherichia coli
2.3.1.180 7-[(1E)-nonadec-1-en-1-yl]-3,4-dihydro-2H-1,5-benzodioxepine
-
 Escherichia coli
2.3.1.180 acetoxyanthecotulide
-
 Escherichia coli
2.3.1.180 anthecotulide
-
 Escherichia coli
2.3.1.180 ethyl (2Z)-2-[4-(benzyloxy)phenyl]-3-[(4-methylphenyl)amino]prop-2-enoate displays effective FabH inhibitory activity and excellent antibacterial activity against Gram-negative Escherichia coli. Binds to FabH through two interactions: a hydrogen bond between the N-H group and the side chain carbonyl group of Gly 209 and a hydro Escherichia coli
2.3.1.180 hydroxyanthecotulide
-
 Escherichia coli
2.3.1.180 kanamycin
-
 Bacillus subtilis
2.3.1.180 kanamycin
-
 Escherichia coli
2.3.1.180 kanamycin
-
 Pseudomonas aeruginosa
2.3.1.180 kanamycin
-
 Staphylococcus aureus
2.3.1.180 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 Bacillus subtilis
2.3.1.180 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. Aryl-alkyl disulfide derivatives can selectively inhibit FabH by reversibly capping the active-site cysteine through a thioldisulfide exchange Escherichia coli
2.3.1.180 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. No inhibition of the enzyme FabH from Mycobacterium tuberculosis by methyl 2-amino-5-benzylthiazole-4-carboxylate Haemophilus influenzae
2.3.1.180 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. No inhibition of the enzyme FabH from Mycobacterium tuberculosis by methyl 2-amino-5-benzylthiazole-4-carboxylate Mycobacterium tuberculosis
2.3.1.180 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 Pseudomonas aeruginosa
2.3.1.180 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
2.3.1.180 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. No inhibition of the enzyme FabH from Mycobacterium tuberculosis by methyl 2-amino-5-benzylthiazole-4-carboxylate Streptococcus pneumoniae
2.3.1.180 N'-[(E)-(3,5-dibromo-2,4-dihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
-
 Escherichia coli
2.3.1.180 N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-hydroxy-3-methoxybenzohydrazide
-
 Escherichia coli
2.3.1.180 N-(3-(5-bromo-2-hydroxybenzylideneamino)propyl)-2-hydroxybenzamide
-
 Escherichia coli
2.3.1.180 SB-418011
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Streptococcus pneumoniae
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Staphylococcus aureus
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Mycobacterium tuberculosis
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Escherichia coli
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Pseudomonas aeruginosa
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Bacillus subtilis
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Haemophilus influenzae
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Staphylococcus aureus N315
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Mycobacterium tuberculosis H37Rv
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.179 Enterococcus faecalis
-
-
-
2.3.1.179 Haemophilus influenzae
-
-
-
2.3.1.179 Staphylococcus aureus
-
-
-
2.3.1.180 Bacillus subtilis O34746 gene fabH
-
2.3.1.180 Escherichia coli P0A6R0 gene fabH
-
2.3.1.180 Haemophilus influenzae P43711 gene fabH
-
2.3.1.180 Mycobacterium tuberculosis P9WNG3 gene fabH
-
2.3.1.180 Mycobacterium tuberculosis H37Rv P9WNG3 gene fabH
-
2.3.1.180 Pseudomonas aeruginosa A0A072ZQE7 gene fabH
-
2.3.1.180 Staphylococcus aureus P99159 gene fabH
-
2.3.1.180 Staphylococcus aureus N315 P99159 gene fabH
-
2.3.1.180 Streptococcus pneumoniae P0A3C5 gene fabH
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.179 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
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Streptococcus pneumoniae
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Staphylococcus aureus
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Mycobacterium tuberculosis
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Escherichia coli
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Pseudomonas aeruginosa
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Bacillus subtilis
a
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2 the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism Haemophilus influenzae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Streptococcus pneumoniae an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Staphylococcus aureus an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Mycobacterium tuberculosis an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Escherichia coli an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Pseudomonas aeruginosa an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Bacillus subtilis an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Haemophilus influenzae an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] the enzyme shows a high selectivity for acetyl-CoA over acyl-ACP as its substrate. Escherichia coli FabH is inactive for longer-chain (greater than C4) primers and all branched-chain CoA primers Escherichia coli an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Staphylococcus aureus N315 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Mycobacterium tuberculosis H37Rv an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.180 More FabH has a catalytic triad of Cys112/His244/Asn274 Staphylococcus aureus
2.3.1.180 More FabH has a catalytic triad of Cys112/His244/Asn274 Escherichia coli
2.3.1.180 More FabH has a catalytic triad of Cys112/His244/Asn274 Pseudomonas aeruginosa
2.3.1.180 More FabH has a catalytic triad of Cys112/His244/Asn274 Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
2.3.1.179 FASII
-
 Staphylococcus aureus
2.3.1.179 FASII
-
 Haemophilus influenzae
2.3.1.179 FASII
-
 Enterococcus faecalis
2.3.1.179 fatty acid synthesis type II
-
 Staphylococcus aureus
2.3.1.179 fatty acid synthesis type II
-
 Haemophilus influenzae
2.3.1.179 fatty acid synthesis type II
-
 Enterococcus faecalis
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Streptococcus pneumoniae
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Staphylococcus aureus
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Mycobacterium tuberculosis
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Escherichia coli
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Pseudomonas aeruginosa
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Bacillus subtilis
2.3.1.180 beta-ketoacyl-ACP synthase III
-
 Haemophilus influenzae
2.3.1.180 FabH
-
 Streptococcus pneumoniae
2.3.1.180 FabH
-
 Staphylococcus aureus
2.3.1.180 FabH
-
 Mycobacterium tuberculosis
2.3.1.180 FabH
-
 Escherichia coli
2.3.1.180 FabH
-
 Pseudomonas aeruginosa
2.3.1.180 FabH
-
 Bacillus subtilis
2.3.1.180 FabH
-
 Haemophilus influenzae

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.180 acetyl-CoA
-
 Streptococcus pneumoniae
2.3.1.180 acetyl-CoA
-
 Staphylococcus aureus
2.3.1.180 acetyl-CoA
-
 Mycobacterium tuberculosis
2.3.1.180 acetyl-CoA
-
 Escherichia coli
2.3.1.180 acetyl-CoA
-
 Pseudomonas aeruginosa
2.3.1.180 acetyl-CoA
-
 Bacillus subtilis
2.3.1.180 acetyl-CoA
-
 Haemophilus influenzae

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.3.1.180 0.00088
-
 pH and temperature not specified in the publication Escherichia coli N-(3-(5-bromo-2-hydroxybenzylideneamino)propyl)-2-hydroxybenzamide
2.3.1.180 0.0018
-
 pH and temperature not specified in the publication Escherichia coli 4-[(1Z)-N,2-bis(4-chlorophenyl)ethanimidoyl]benzene-1,3-diol
2.3.1.180 0.0021
-
 pH and temperature not specified in the publication Escherichia coli N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-hydroxy-3-methoxybenzohydrazide
2.3.1.180 0.0025
-
 pH and temperature not specified in the publication Escherichia coli 1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl (2E)-3-(biphenyl-4-yl)prop-2-enoate
2.3.1.180 0.0026
-
 pH and temperature not specified in the publication Escherichia coli ethyl (2Z)-2-[4-(benzyloxy)phenyl]-3-[(4-methylphenyl)amino]prop-2-enoate
2.3.1.180 0.0027
-
 pH and temperature not specified in the publication Escherichia coli 4-fluoro-2-[(E)-[[2-(4-hydroxyphenyl)ethyl]imino]methyl]phenol
2.3.1.180 0.0036
-
 pH and temperature not specified in the publication Escherichia coli 2,4-dibromo-6-[(E)-[2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]phenol
2.3.1.180 0.0042
-
 pH and temperature not specified in the publication Escherichia coli 1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
2.3.1.180 0.0043
-
 pH and temperature not specified in the publication Escherichia coli 1-(4-[(E)-[3-(benzyloxy)benzylidene]amino]phenyl)-3-phenylthiourea
2.3.1.180 0.0043
-
 pH and temperature not specified in the publication Escherichia coli 2-(2-methoxyphenyl)-5-[(2-methyl-5-nitro-1H-imidazol-1-yl)methyl]-1,3,4-oxadiazole
2.3.1.180 0.0046
-
 pH and temperature not specified in the publication Escherichia coli 2-[3-(3,4-dichlorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
2.3.1.180 0.0047
-
 pH and temperature not specified in the publication Escherichia coli 1-(5-bromo-2-hydroxybenzyl)-1-(4-chlorophenyl)-3-phenylurea

General Information

EC Number General Information Comment Organism
2.3.1.179 physiological function fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis Staphylococcus aureus
2.3.1.179 physiological function fatty acid synthesis type II system enzymes are essential for bacterial membrane lipid biosynthesis Haemophilus influenzae
2.3.1.179 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
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Streptococcus pneumoniae
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Staphylococcus aureus
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Mycobacterium tuberculosis
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Escherichia coli
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Pseudomonas aeruginosa
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Bacillus subtilis
2.3.1.180 evolution FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa Haemophilus influenzae
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Streptococcus pneumoniae
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Staphylococcus aureus
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Mycobacterium tuberculosis
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Escherichia coli
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Pseudomonas aeruginosa
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Bacillus subtilis
2.3.1.180 metabolism FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview Haemophilus influenzae
2.3.1.180 additional information FabH has a catalytic triad of Cys112/His244/Asn274 Streptococcus pneumoniae
2.3.1.180 additional information FabH has a catalytic triad of Cys112/His244/Asn274 Staphylococcus aureus
2.3.1.180 additional information FabH has a catalytic triad of Cys112/His244/Asn274 Mycobacterium tuberculosis
2.3.1.180 additional information FabH has a catalytic triad of Cys112/His244/Asn274 Pseudomonas aeruginosa
2.3.1.180 additional information FabH has a catalytic triad of Cys112/His244/Asn274 Bacillus subtilis
2.3.1.180 additional information FabH has a catalytic triad of Cys112/His244/Asn274 Haemophilus influenzae
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Streptococcus pneumoniae
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Staphylococcus aureus
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Mycobacterium tuberculosis
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Escherichia coli
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Pseudomonas aeruginosa
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Bacillus subtilis
2.3.1.180 physiological function enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway Haemophilus influenzae