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Information on EC 2.3.1.180 - beta-ketoacyl-[acyl-carrier-protein] synthase III
for references in articles please use BRENDA:EC2.3.1.180
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.180 beta-ketoacyl-[acyl-carrier-protein] synthase III
IUBMB Comments
The enzyme is responsible for initiating straight-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. In contrast to EC 2.3.1.41, β-ketoacyl-[acyl-carrier-protein] synthase I, and EC 2.3.1.179, β-ketoacyl-[acyl-carrier-protein] synthase II, this enzyme specifically uses short-chain acyl-CoA thioesters (preferably acetyl-CoA) rather than acyl-[acp] as its substrate . The enzyme can also catalyse the reaction of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much lesser extent . The enzymes from some organisms (e.g. the Gram-positive bacterium Streptococcus pneumoniae) can accept branched-chain acyl-CoAs in addition to acetyl-CoA (cf. EC 2.3.1.300, branched-chain β-ketoacyl-[acyl-carrier-protein] synthase).
The enzyme appears in viruses and cellular organisms
- 2.3.1.180
- malonyl-acp
- thiolactomycin
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transacylase
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mycolic
- drug development
- acyl-acps
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claisen
- glaucescens
- isobutyryl-coa
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transacylation
- cuphea
- pharmacology
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malonyl-coa:acp
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bcfas
- synthesis
- biofuel production
- medicine
Reaction Schemes
showSynonyms
kas iii, mtfabh, kasiii, beta-ketoacyl-acyl carrier protein synthase iii, pqsbc, beta-ketoacyl-acyl carrier protein (acp) synthase iii, beta-ketoacyl-acp synthase iii, ecfabh, acetoacetyl-acp synthase, 3-ketoacyl-acyl carrier protein synthase iii, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl ACP synthase III
3-ketoacyl ACP synthetase III
3-ketoacyl acyl carrier protein synthase III
3-ketoacyl-ACP synthase III
3-ketoacyl-acyl carrier protein synthase III
3-ketoacyl-acyl-carrier protein synthase III
3-oxoacyl-ACP synthase III
3-oxoacyl-acyl carrier protein synthase III
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3-oxoacyl:ACP synthase III
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AbyA1
acetoacetyl-ACP synthase
acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase
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ACP synthase III
AknE2
AsuC3
AsuC4
AviN
beta-ketoacyl acyl carrier protein synthase III
beta-ketoacyl-(ACP) synthase III
beta-ketoacyl-ACP synthase
beta-ketoacyl-ACP synthase III
beta-ketoacyl-ACP synthase-like acyltransferase
beta-ketoacyl-ACP-synthase III
beta-ketoacyl-acyl carrier protein synthase III
beta-ketoacyl-[acyl-carrier-protein] synthase III
CalO4
CerJ
ChlB3
CorB
DarB
FabH
FabH1
FabH2
FabHA
FabHB
FdmS
FrenI/FrnI
initiation ketosynthase
KAS III
KAS-III
KASIII
KijB
KSIII
MxnB
PpyS
PtmR
RedP
SalQ/Orf12
SCO6564
spyFabH
ThgI
TiaF
beta-ketoacyl-acyl carrier protein synthase III
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beta-ketoacyl-acyl carrier protein synthase III
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beta-ketoacyl-acyl carrier protein synthase III
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beta-ketoacyl-acyl carrier protein synthase III
also catalyzing acetyl-CoA:ACP transacylase reaction
beta-ketoacyl-acyl carrier protein synthase III
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FabH
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FabH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
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-
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
ping pong reaction mechanism, catalysis involves His261, Arg150, and Arg306, determination of substrate binding site
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism via a tetrahedral transition state, active site structure contains an oxyanion hole and a tunnel, catalytic residues are Cys112, His244, and Asn274, which are all required for condensation activity of the enzyme, additionally His244 and Asp274 are required for decarboxylation, Cys112 is essential for transacylation, overview
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
active site structure a catayltic triad of Cys-His-Asn residues
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
active site structure with a CoA/malonyl-ACP-binding channel leading from the enzyme surface to the buried active site Cys residue, a second channel leads from the active site to the surface with a threonine residue controlling the passage of longer acyl chains
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism might include a water molecule or a hydroxyl anion in Cys112 deprotonation, large conformational changes in the active site e.g. through disordering of four essential loops and the movement of the two catalytic residues Cys112 and His244
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic residues are Cys112, His244, and Asn274, catalytic reaction mechanism includes acetylation of Cys112 in the primer binding pocket, structure and reaction mechanism modeling
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
the active site is formed by Ala-Cys-Ala
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
active site structure contains a catalytic triad of His249-Asn279-Cys112 residues
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic residues are Cys123, His323, and Asn353
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
active site structure and catalytic reaction mechanism, T97, R46, W42, C122, R161, H258, and N289 are important for activity, structure-function relationship
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
ping pong reaction mechanism, catalytically important residues are Phe298 and His238
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism for decarboxylation and condensation
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
data support a new model for catalysis, in which FabH exists in an open form that permits binding of the long chain acyl-coenzyme A substrate binding and release of the corresponding 3-ketoacyl ACP product. Catalysis and intermediate steps in the process are proposed to occur in a closed form of the mtFabH. These conformational changes may be critical for binding and dissociation steps in other enzymes of the FAS pathways, including transfers between the type I and type II FASII components of Mycobacterium tuberculosis
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
proposed mechanism of condensation reaction in Streptococcus gordonii FabH between catalytic residues His249, Asn279 and Cys112
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
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
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
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
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
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
two-stage mechanism, driven by a dipole moment, the active site cysteine, Cys112 in YpFabH attacks the acyl group of a fatty acyl donor, transferring the acyl group to the enzyme. The bound fatty acyl donor molecule is displaced, and the receiving molecule or fatty acyl thioester to be elongated binds, initiating the transfer of the acyl group from the condensing enzyme to the recipient. The remaining residues of the catalytic triad, His243 and Asn273, are thought to stabilise the fatty acyl intermediate during transition states
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
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
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
active site structure and catalytic reaction mechanism, T97, R46, W42, C122, R161, H258, and N289 are important for activity, structure-function relationship
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism for decarboxylation and condensation
-
-
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
data support a new model for catalysis, in which FabH exists in an open form that permits binding of the long chain acyl-coenzyme A substrate binding and release of the corresponding 3-ketoacyl ACP product. Catalysis and intermediate steps in the process are proposed to occur in a closed form of the mtFabH. These conformational changes may be critical for binding and dissociation steps in other enzymes of the FAS pathways, including transfers between the type I and type II FASII components of Mycobacterium tuberculosis
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-
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
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-
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
-
-
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism for decarboxylation and condensation
-
-
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
data support a new model for catalysis, in which FabH exists in an open form that permits binding of the long chain acyl-coenzyme A substrate binding and release of the corresponding 3-ketoacyl ACP product. Catalysis and intermediate steps in the process are proposed to occur in a closed form of the mtFabH. These conformational changes may be critical for binding and dissociation steps in other enzymes of the FAS pathways, including transfers between the type I and type II FASII components of Mycobacterium tuberculosis
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
proposed mechanism of condensation reaction in Streptococcus gordonii FabH between catalytic residues His249, Asn279 and Cys112
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
fatty acid biosynthesis initiation (type II), streptorubin B biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
The enzyme is responsible for initiating straight-chain fatty acid biosynthesis by the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. In contrast to EC 2.3.1.41, beta-ketoacyl-[acyl-carrier-protein] synthase I, and EC 2.3.1.179, beta-ketoacyl-[acyl-carrier-protein] synthase II, this enzyme specifically uses short-chain acyl-CoA thioesters (preferably acetyl-CoA) rather than acyl-[acp] as its substrate [1]. The enzyme can also catalyse the reaction of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, but to a much lesser extent [1]. The enzymes from some organisms (e.g. the Gram-positive bacterium Streptococcus pneumoniae) can accept branched-chain acyl-CoAs in addition to acetyl-CoA [5] (cf. EC 2.3.1.300, branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase).
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CAS REGISTRY NUMBER
COMMENTARY
9077-10-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E)-oct-2-enethioyl-CoA + (3S,5Z,8Z)-3-hydroxytetradeca-5,8-dienoyl-CoA
(3S,5S,7Z,10Z)-2-hexyl-3,5-dihydroxyhexadeca-7,10-dienoic acid + ?
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Substrates: -
Products: -
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?
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
2-methylcrotonyl-CoA + malonyl-[acyl-carrier protein]
(4E)-4-methylhex-4-enoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
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?
3-oxoacyl-ACP + acetyl-CoA
acetyl-ACP + 3-ketoacyl-CoA
-
Substrates: -
Products: -
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?
6-methylsalicyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
6-methylsalicyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
acetoacetyl-ACP + acetyl-CoA
acetyl-ACP + acetoacetyl-CoA
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Substrates: -
Products: -
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?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + ACP
acetyl-ACP + CoA
Substrates: acetyl-CoA:ACP transacylase activity
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutyryl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + [acyl-carrier protein]
acetyl-[acyl-carrier protein] + CoA
Substrates: the enzyme also shows acetyltransferase activity
Products: -
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?
acetyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
acetoacetyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
acyl-CoA + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CoA + CO2
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Substrates: the reaction is catalyzed by isoform FabH2
Products: -
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?
arachidoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-docosanoyl-[acyl-carrier protein] + CoA + CO2
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Substrates: low activity
Products: -
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?
butanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexanoyl-[acyl-carrier protein] + CoA + CO2
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
butyryl-CoA + malonyl-[acyl-carrier protein]
hexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
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?
cyclohexanecarboxyl-CoA + malonyl-[acyl-carrier protein AsuC5]
3-oxocyclohexylpropyl-[acyl-carrier protein AsuC5] + CoA + CO2
-
Substrates: -
Products: -
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?
cyclohexonyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
cyclohexonyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) (2E)-2,4-dimethylpent-2-enethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl (3E)-3,5-dimethylhex-3-enoate + N-(2-sulfanylethyl)acetamide
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Substrates: 44% conversion
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) 2-hydroxy-6-methylbenzene-1-carbothioate
7-deoxy-7-demethylpactamycin + N-(2-sulfanylethyl)acetamide
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Substrates: 100% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) 2-methylbutanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl 2-methylbutanoate + N-(2-sulfanylethyl)acetamide
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Substrates: 20% conversion
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) 2-methylpropanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl 2-methylpropanoate + N-(2-sulfanylethyl)acetamide
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Substrates: 83% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) 3-aminobenzene-1-carbothioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl 3-aminobenzoate + N-(2-sulfanylethyl)acetamide
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Substrates: 17% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) 3-methylbutanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl 3-methylbutanoate + N-(2-sulfanylethyl)acetamide
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Substrates: 61% conversion
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) 4-chlorobutanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl 4-chlorobutanoate + N-(2-sulfanylethyl)acetamide
-
Substrates: 100% conversion
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) benzenecarbothioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl benzoate + N-(2-sulfanylethyl)acetamide
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Substrates: 43% conversion
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) butanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl butanoate + N-(2-sulfanylethyl)acetamide
-
Substrates: 91% conversion
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) cycloheptanecarbothioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl cycloheptanecarboxylate + N-(2-sulfanylethyl)acetamide
-
Substrates: 87% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) cyclohexanecarbothioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl cyclohexanecarboxylate + N-(2-sulfanylethyl)acetamide
-
Substrates: 57% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) ethanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl acetate + N-(2-sulfanylethyl)acetamide
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Substrates: 71% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) phenylethanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl phenylacetate + N-(2-sulfanylethyl)acetamide
-
Substrates: 95% conversion
Products: -
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?
de-(6-methylsalicylyl)-7-deoxy-7-demethylpactamycin + S-(2-acetamidoethyl) propanethioate
[(1S,2R,3S,4S,5S)-5-(3-acetylanilino)-4-amino-3-[(dimethylcarbamoyl)amino]-1,2-dihydroxy-2,3-dimethylcyclopentyl]methyl propanoate + N-(2-sulfanylethyl)acetamide
-
Substrates: 87% conversion
Products: -
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?
de-6-methylsalicylyl-7-deoxypactamycin + 6-methylsalicylyl N-acetylcysteamine thioester
?
-
Substrates: -
Products: -
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?
de-6-methylsalicylyl-pactamycate + 6-methylsalicylyl N-acetylcysteamine thioester
?
-
Substrates: -
Products: -
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?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-lauroyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
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?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxododecanoyl-[acyl-carrier protein] + CoA + CO2
heptanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-nonanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-octanoyl-[acyl-carrier protein] + CoA + CO2
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CoA + CO2
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methyl-pentanoyl-[acyl-carrier protein] + CoA + CO2
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylpentanoyl-[acyl-carrier protein] + CoA + CO2
isobutyryl-CoA + malonyl-[acyl-carrier protein]
isohexanoyl-[acyl-carrier protein] + CoA + CO2
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methyl-hexanoyl-[acyl-carrier protein] + CoA + CO2
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
isovaleryl-CoA + malonyl-[acyl-carrier protein]
isoheptanoyl-[acyl-carrier protein] + CoA + CO2
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2
malonyl-ACP + acyl-CoA
3-oxoacyl-ACP + CoA + CO2
Substrates: specificity for branched acyl-CoA substrate
Products: -
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?
malonyl-ACP + acyl-CoA
CO2 + CoA + ?
Substrates: -
Products: -
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?
malonyl-[ACP] + acetyl-CoA + H+
3-oxobutanoyl-[ACP] + CO2 + CoA
Substrates: -
Products: -
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?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-palmitoyl-[acyl-carrier protein] + CoA + CO2
octanoyl-CoA + (3S,5Z,8Z)-3-hydroxytetradeca-5,8-dienoyl-CoA
(5S,7Z,10Z)-2-hexyl-5-hydroxy-3-oxohexadeca-7,10-dienoic acid + ?
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-decanoyl-[acyl-carrier protein] + CoA + CO2
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
palmitoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-stearoyl-[acyl-carrier protein] + CoA + CO2
propanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopentanoyl-[acyl-carrier-protein] + CoA + CO2
propionyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-valeryl-[acyl-carrier protein] + CoA + CO2
stearoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-arachidoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: low activity
Products: -
Products: -
?
valeryl-CoA + malonyl-[acyl-carrier protein]
3-oxoheptanoyl-[acyl-carrier-protein] + CoA + CO2
[PtmQ]-S-methyl 2-methylbenzene-1-carbothioate + de-6-methylsalicylyl-pactamycin
pactamycin + ?
-
Substrates: -
Products: -
Products: -
?
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: 2-methylbutyryl-CoA is the preferred substrate
Products: -
Products: -
?
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
6-methylsalicyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
6-methylsalicyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
Substrates: highest activity
Products: -
Products: -
?
6-methylsalicyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
6-methylsalicyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
Streptomyces antibioticus DSM-40725
Substrates: highest activity
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: 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
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Myxococcus fulvus Mxf50
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Polymorphospora rubra K07-0510
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Pseudomonas putida BW11M1
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces albus XM211
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces antibioticus DSM 4072
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces antibioticus Tue2706
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces galilaeus 3AR-33
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces griseus ATCC 49344
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces roseofulvus AM-3867
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces sp. MA347
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces tendae HKI 017
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
B1XPH5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
B1XPH5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-ACP
acetoacetyl-ACP + CoA + CO2
Substrates: ACP acceptor substrates with eight carbons and potentially also with ten carbons are used, substrate specificity is not limited to using C2-CoA
Products: -
Products: -
?
acetyl-CoA + malonyl-ACP
acetoacetyl-ACP + CoA + CO2
Substrates: ACP acceptor substrates with eight carbons and potentially also with ten carbons are used, substrate specificity is not limited to using C2-CoA
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutyryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH1
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutyryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH1
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: first condensing step in fatty acid synthase reaction, the enzyme is feedback regulated in biosynthesis of medium chain fatty acids
Products: -
Products: -
r
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: regulation of the enzyme activity is involved in regulation of fatty acid synthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: regulation of the enzyme activity is involved in regulation of the fatty acid synthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: regulation by feedback inhibition
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme catalyzes the initial step in fatty acid biosynthesis via type II fatty acid synthase
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: initial condensation reaction to start fatty acid biosynthesis by the type II fatty acid synthase, the enzyme is a target for fatty acid synthesis regulation by acyl-[acyl-carrier-protein]
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: acetyl-CoA and propionyl-CoA are the preferred primers
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
r
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme is essential for fatty acid biosynthesis, especially of short-chain fatty acids, by fatty acid synthase II initiating the elongation of fatty acids
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme is essential for fatty acid biosynthesis, especially of short-chain fatty acids, by fatty acid synthase II initiating the elongation of fatty acids
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: condensation of fatty acid synthase I-derived acyl-CoAs with malonyl-ACPs to initiates fatty acid synthase II-catalyzed fatty acid elongation, the enzyme links the two fatty acid synthase complexes
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: condensation of fatty acid synthase I-derived acyl-CoAs with malonyl-ACPs to initiates fatty acid synthase II-catalyzed fatty acid elongation, the enzyme links the two fatty acid synthase complexes
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
r
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme is involved in initiation of fatty acid elogantion by the fatty acid synthase II catalyzing the decarboxylative condensation between malonyl-ACP and acetyl-CoA, the enzyme is essential for viability, overview
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme catalyzes the initial step in fatty acid biosynthesis via type II fatty acid synthase
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: low activity
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: preferred CoA primer is acetyl-CoA
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis, overview
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: FabH initiates the elongation of straight-chain fatty acids by the fatty acid synthase II complex, fatty acid synthesis pathway overview
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: substrate malonyl-ACP is produced by FabC or Escherichia coli AcpP, but not by TcmM
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
butyryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
butyryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
acetoacetyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
Substrates: -
Products: -
Products: -
?
acetyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
acetoacetyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
Streptomyces antibioticus DSM-40725
Substrates: -
Products: -
Products: -
?
acyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the condensation reaction is the first step in elongation in fatty acid synthesis by fatty acid synthase complex
Products: -
Products: -
?
acyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme prefers long-chain fatty acids
Products: -
Products: -
?
butanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
butanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier-protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
cyclohexonyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
cyclohexonyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
Substrates: -
Products: -
Products: -
?
cyclohexonyl-N-acetylcysteamine + malonyl-[acyl-carrier protein ChlB2]
cyclohexonyl-[acyl-carrier protein ChlB2] + N-acetylcysteamine + CO2
Streptomyces antibioticus DSM-40725
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxododecanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxododecanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-octanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-octanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-octanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: high activity
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
octanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + malonyl-[acyl-carrier protein]
octanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methyl-pentanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: isobutyryl-CoA is the preferred CoA primer substrate
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methyl-pentanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: isobutyryl-CoA is the preferred primer substrate
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methyl-pentanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methyl-pentanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylpentanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylpentanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
isohexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
isohexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methyl-hexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methyl-hexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
isovaleryl-CoA + malonyl-[acyl-carrier protein]
isoheptanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isovaleryl-CoA + malonyl-[acyl-carrier protein]
isoheptanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: lauroyl-CoA is the preferred primer
Products: -
Products: -
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2
Substrates: the primer substrate lauroyl-CoA is bound to subunit A, binding structure, lauroyl is bound in a channel
Products: -
Products: -
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the primer substrate lauroyl-CoA is bound to subunit A, binding structure, lauroyl is bound in a channel
Products: -
Products: -
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2
Substrates: the primer substrate lauroyl-CoA is bound to subunit A, binding structure, lauroyl is bound in a channel
Products: -
Products: -
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-myristoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
malonyl-ACP + acetyl-CoA
CO2 + CoA + acetoacetyl-ACP
-
Substrates: -
Products: -
Products: -
?
malonyl-ACP + acetyl-CoA
CO2 + CoA + acetoacetyl-ACP
Substrates: -
Products: -
Products: -
?
malonyl-ACP + acetyl-CoA
CO2 + CoA + acetoacetyl-ACP
Substrates: -
Products: -
Products: -
?
malonyl-ACP + acetyl-CoA
CO2 + CoA + acetoacetyl-ACP
Substrates: -
Products: -
Products: -
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-palmitoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme plays a key role in initiation of the long-chain fatty acid route of meromycolic acid biosynthesis, a different enzyme with specificity for short-chain acyl-CoAs might also be responsible for meromycolic acid biosynthesis, biosynthetic pathway regulation mechanism
Products: -
Products: -
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-palmitoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-palmitoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme prefers long-chain acyl-CoA substrates for the Claisen condensation reaction
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-decanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-decanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the reaction is strongly catalyzed by isoform FabH2 and weakly catalyzed by isoform FabH1
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
decanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
decanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
decanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-stearoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-stearoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
propanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopentanoyl-[acyl-carrier-protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
propanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopentanoyl-[acyl-carrier-protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
propionyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-valeryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: acetyl-CoA and propionyl-CoA are the preferred primers
Products: -
Products: -
?
propionyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-valeryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
propionyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-valeryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme specifies the propionate-starter unit for type II polyketide biosynthesis
Products: -
Products: -
?
propionyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-valeryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: intermediate binding of propionyl to the enzyme at Ser118
Products: -
Products: -
?
valeryl-CoA + malonyl-[acyl-carrier protein]
3-oxoheptanoyl-[acyl-carrier-protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
valeryl-CoA + malonyl-[acyl-carrier protein]
3-oxoheptanoyl-[acyl-carrier-protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: fatty acid composition and acyl-ACP content in the seeds
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural and dynamical aspect of catalytic mechanism of FabH, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is important in fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is important in fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is important in fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a key catalyst of fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild-type enzyme is able to induce synthesis of polyhydroxyalkanoates PHA copolymers from glucose in a strain which is transformed with gene phaC from Aeromonas caviae or gene phaC1 from Pseudomonas sp. strain 61-3, thus fatty acid biosynthesis may supply monomers for PHA production, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows also acyl-CoA-[acyl-carrier-protein] transacylase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with hexanoyl-CoA or octanoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows also acyl-CoA-[acyl-carrier-protein] transacylase activity
Products: -
Products: -
?
additional information
?
-
Substrates: substrate binding channel at the active site, structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding channel at the active site, structure, overview
Products: -
Products: -
?
additional information
?
-
Substrates: FabH catalyzes the initial step of fatty acid biosynthesis via a type II fatty acid synthase, FabH has an important role as essential enzyme combined with unique structural features and ubiquitous occurrence
Products: -
Products: -
?
additional information
?
-
-
Substrates: FabH catalyzes the initial step of fatty acid biosynthesis via a type II fatty acid synthase, FabH has an important role as essential enzyme combined with unique structural features and ubiquitous occurrence
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is essential for fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
Lactiplantibacillus plantarum ATCC BAA-793
Substrates: the enzyme is essential for fatty acid biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers short-chain CoA primer substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme prefers short-chain CoA primer substrates
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows also acetyl-CoA-[acyl-carrier-protein] transacylase activity
Products: -
Products: -
?
additional information
?
-
Substrates: beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
Products: -
Products: -
?
additional information
?
-
-
Substrates: beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, FabH has a clear preference for branched-chain CoA precursors versus acetyl-CoA at 30°C, while this preference is not so pronounced at 10°C, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, FabH has a clear preference for branched-chain CoA precursors versus acetyl-CoA at 30°C, while this preference is not so pronounced at 10°C, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, no activity with isovaleryl-CoA, butyryl-CoA, and acetyl-CoA, the enzyme prefers long chain acyl-CoAs as primers rather than acyl-ACPs
Products: -
Products: -
?
additional information
?
-
Substrates: specificity of the enzyme for longer acyl-CoA chains, overview, the enzyme shows also acyl-CoA-[acyl-carrier-protein] transacylase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity of the enzyme for longer acyl-CoA chains, overview, the enzyme shows also acyl-CoA-[acyl-carrier-protein] transacylase activity
Products: -
Products: -
?
additional information
?
-
Substrates: FabH is regulated by Ser/Thr protein kinase-dependent phosphorylation at Thr45, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: FabH is regulated by Ser/Thr protein kinase-dependent phosphorylation at Thr45, overview
Products: -
Products: -
?
additional information
?
-
Substrates: specificity of the enzyme for longer acyl-CoA chains, overview, the enzyme shows also acyl-CoA-[acyl-carrier-protein] transacylase activity
Products: -
Products: -
?
additional information
?
-
Substrates: FabH is regulated by Ser/Thr protein kinase-dependent phosphorylation at Thr45, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: fatty acid composition and acyl-ACP content in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding channel at the active site, structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding channel at the active site, structure, overview
Products: -
Products: -
?
additional information
?
-
Substrates: fatty acid composition and acyl-ACP content in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: fatty acid composition and acyl-ACP content in the leaves
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, the enzyme also shows acetyltransferase activity, which is lower than the 3-ketoacyl carrier protein synthase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme possesses a large primer binding pocket determining the substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, the recombinant enzyme prefers straight short-chain CoA primer substrates, preferred CoA primer is acetyl-CoA, no activity with lauroyl-CoA and palmitoyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, the recombinant enzyme prefers straight short-chain CoA primer substrates, preferred CoA primer is acetyl-CoA, no activity with lauroyl-CoA and palmitoyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is responsible for the initiation of fatty acid biosynthesis and for viability
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is responsible for the initiation of fatty acid biosynthesis and for viability
Products: -
Products: -
?
additional information
?
-
-
Substrates: fatty acid composition of wild-type and mutant strains, the latter expressing plasmid-encoded Escherichia coli or Streptomyces glaucescens enzymes, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is not directly involved in tetracenomycin C biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of straight-chain and branched-chain fatty acids with the specificity for acyl-CoA substrate determining the produced fatty acid spectrum
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows also acyl-CoA:[acyl-carrier-protein] transacylase activity, i.e. ACAT activity, in a ratio of 1:0.12 with beta-oxoacyl-[acyl-carrier-protein] synthase III activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with acetyl-CoA, malonyl-CoA, and 2-methylmalonyl-CoA as primer for elongation of fatty acids, the enzyme shows also acyl-CoA:ACP transacylase activity for transfer of propionate to ACP
Products: -
Products: -
?
additional information
?
-
B1XPH5
Substrates: Product profile analysis of FabH from Synechococcus sp. strain PCC 7002, overview. t´The major products are lauric acid, myristic acid, palmitic acid, and stearic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: Product profile analysis of FabH from Synechococcus sp. strain PCC 7002, overview. t´The major products are lauric acid, myristic acid, palmitic acid, and stearic acid
Products: -
Products: -
?
additional information
?
-
B1XPH5
Substrates: Product profile analysis of FabH from Synechococcus sp. strain PCC 7002, overview. t´The major products are lauric acid, myristic acid, palmitic acid, and stearic acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure-function relationship, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has a preferance for using branched chain acyl-CoAs as primers and also displays a strong activity towards short or medium chain acyl-CoAs (about C4-C10)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also exhibits acyl-CoA:ACP transacylase activity
Products: -
Products: -
-
additional information
?
-
-
Substrates: structure-function relationship, overview
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme substrate specificity, overview
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methyl-pentanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylpentanoyl-[acyl-carrier protein] + CoA + CO2
isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
malonyl-[ACP] + acetyl-CoA + H+
3-oxobutanoyl-[ACP] + CO2 + CoA
Substrates: -
Products: -
Products: -
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-palmitoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme plays a key role in initiation of the long-chain fatty acid route of meromycolic acid biosynthesis, a different enzyme with specificity for short-chain acyl-CoAs might also be responsible for meromycolic acid biosynthesis, biosynthetic pathway regulation mechanism
Products: -
Products: -
?
propionyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-valeryl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme specifies the propionate-starter unit for type II polyketide biosynthesis
Products: -
Products: -
?
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
2-methylbutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Myxococcus fulvus Mxf50
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Polymorphospora rubra K07-0510
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Pseudomonas putida BW11M1
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces albus XM211
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces antibioticus DSM 4072
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces antibioticus Tue2706
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces galilaeus 3AR-33
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces griseus ATCC 49344
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces roseofulvus AM-3867
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces sp. MA347
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Streptomyces tendae HKI 017
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
B1XPH5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
B1XPH5
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + a malonyl-[acyl-carrier protein]
an acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: first condensing step in fatty acid synthase reaction, the enzyme is feedback regulated in biosynthesis of medium chain fatty acids
Products: -
Products: -
r
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: regulation of the enzyme activity is involved in regulation of fatty acid synthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: regulation of the enzyme activity is involved in regulation of the fatty acid synthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: regulation by feedback inhibition
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme catalyzes the initial step in fatty acid biosynthesis via type II fatty acid synthase
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: initial condensation reaction to start fatty acid biosynthesis by the type II fatty acid synthase, the enzyme is a target for fatty acid synthesis regulation by acyl-[acyl-carrier-protein]
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
r
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme is essential for fatty acid biosynthesis, especially of short-chain fatty acids, by fatty acid synthase II initiating the elongation of fatty acids
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme is essential for fatty acid biosynthesis, especially of short-chain fatty acids, by fatty acid synthase II initiating the elongation of fatty acids
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: condensation of fatty acid synthase I-derived acyl-CoAs with malonyl-ACPs to initiates fatty acid synthase II-catalyzed fatty acid elongation, the enzyme links the two fatty acid synthase complexes
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis
Products: -
Products: -
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: condensation of fatty acid synthase I-derived acyl-CoAs with malonyl-ACPs to initiates fatty acid synthase II-catalyzed fatty acid elongation, the enzyme links the two fatty acid synthase complexes
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: the enzyme initiates the fatty acid biosynthesis
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme is involved in initiation of fatty acid elogantion by the fatty acid synthase II catalyzing the decarboxylative condensation between malonyl-ACP and acetyl-CoA, the enzyme is essential for viability, overview
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme catalyzes the initial step in fatty acid biosynthesis via type II fatty acid synthase
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the enzyme initiates the fatty acid biosynthesis, overview
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: FabH initiates the elongation of straight-chain fatty acids by the fatty acid synthase II complex, fatty acid synthesis pathway overview
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acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: -
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acyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CoA + CO2
-
Substrates: the condensation reaction is the first step in elongation in fatty acid synthesis by fatty acid synthase complex
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acyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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butyryl-CoA + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylpentanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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isobutyryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-4-methylpentanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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isovaleryl-CoA + malonyl-[acyl-carrier protein]
3-oxo-5-methylhexanoyl-[acyl-carrier protein] + CoA + CO2
Substrates: -
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additional information
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-
-
Substrates: fatty acid composition and acyl-ACP content in the seeds
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additional information
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-
Substrates: the enzyme is important in fatty acid biosynthesis
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additional information
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-
-
Substrates: the enzyme is important in fatty acid biosynthesis
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additional information
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-
-
Substrates: the enzyme is important in fatty acid biosynthesis
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additional information
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-
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Substrates: the enzyme is a key catalyst of fatty acid biosynthesis
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additional information
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Substrates: the wild-type enzyme is able to induce synthesis of polyhydroxyalkanoates PHA copolymers from glucose in a strain which is transformed with gene phaC from Aeromonas caviae or gene phaC1 from Pseudomonas sp. strain 61-3, thus fatty acid biosynthesis may supply monomers for PHA production, overview
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additional information
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Substrates: FabH catalyzes the initial step of fatty acid biosynthesis via a type II fatty acid synthase, FabH has an important role as essential enzyme combined with unique structural features and ubiquitous occurrence
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additional information
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-
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Substrates: FabH catalyzes the initial step of fatty acid biosynthesis via a type II fatty acid synthase, FabH has an important role as essential enzyme combined with unique structural features and ubiquitous occurrence
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additional information
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Substrates: the enzyme is essential for fatty acid biosynthesis
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additional information
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-
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Substrates: the enzyme is essential for fatty acid biosynthesis
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additional information
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Lactiplantibacillus plantarum ATCC BAA-793
Substrates: the enzyme is essential for fatty acid biosynthesis
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additional information
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Substrates: the enzyme prefers short-chain CoA primer substrates
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additional information
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Substrates: the enzyme prefers short-chain CoA primer substrates
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additional information
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Substrates: beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
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additional information
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Substrates: beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
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additional information
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-
Substrates: FabH is regulated by Ser/Thr protein kinase-dependent phosphorylation at Thr45, overview
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additional information
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-
-
Substrates: FabH is regulated by Ser/Thr protein kinase-dependent phosphorylation at Thr45, overview
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additional information
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Substrates: FabH is regulated by Ser/Thr protein kinase-dependent phosphorylation at Thr45, overview
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additional information
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-
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Substrates: fatty acid composition and acyl-ACP content in the leaves
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additional information
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-
Substrates: fatty acid composition and acyl-ACP content in the leaves
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additional information
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-
-
Substrates: fatty acid composition and acyl-ACP content in the leaves
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additional information
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-
Substrates: the enzyme is responsible for the initiation of fatty acid biosynthesis and for viability
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additional information
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-
-
Substrates: the enzyme is responsible for the initiation of fatty acid biosynthesis and for viability
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additional information
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-
-
Substrates: fatty acid composition of wild-type and mutant strains, the latter expressing plasmid-encoded Escherichia coli or Streptomyces glaucescens enzymes, overview
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additional information
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Substrates: the enzyme is not directly involved in tetracenomycin C biosynthesis
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additional information
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Substrates: the enzyme is involved in biosynthesis of straight-chain and branched-chain fatty acids with the specificity for acyl-CoA substrate determining the produced fatty acid spectrum
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-bromophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
-
(2-chlorophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
-
(2R)-5-hydroxy-2,4-dimethyl-2-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-3(2H)-one
-
-
(3-bromophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
-
(3-chlorophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
-
(4-bromophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
-
(4-chlorophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
-
(5R)-4-hydroxy-5-[[4'-(hydroxymethyl)biphenyl-4-yl]methyl]-3,5-dimethylthiophen-2(5H)-one
-
-
(5R)-5-[3-(4-acetyl-3-hydroxyphenyl)prop-2-yn-1-yl]-4-hydroxy-3,5-dimethylthiophen-2(5H)-one
-
-
(5R)-5-[3-(4-acetylphenyl)prop-2-yn-1-yl]-4-hydroxy-3,5-dimethylthiophen-2(5H)-one
-
-
(E) -N'-((E)-3-(2-methoxyphenyl)al lyl idene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E) -N'-((E)-3-(2-Ni trophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
(E) -N'-((E)-3-(4-bromophenyl)al lyl idene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(2,4-dichlorophenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(2-bromophenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(3-bromophenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(3-fluorophenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-(benzyloxy)phenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-(dimethylamino)phenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-bromophenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-chlorophenyl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(biphenyl-4-yl)acrylate
-
-
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(naphthalen-1-yl)acrylate
-
-
(E)-1-(6-chloropyridin-3-yl)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methylene)methanamine
-
(E)-1-(6-chloropyridin-3-yl)-N-((3,4-dihydro-2Hbenzo[b][1,4]dioxepin-7-yl)methylene)methanamine
-
(E)-4-chloro-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methylene)pyridin-2-amine
-
(E)-5-chloro-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methylene)pyridin-2-amine
-
(E)-6-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methyleneamino)nicotinonitrile
-
(E)-N'-((E)-3-(2-fluorophenyl)allyl-idene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
-
(E)-N'-((E)-3-(2-methoxyphenyl)allyl-idene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
-
(E)-N'-((E)-3-(2-methoxyphenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
(E)-N'-((E)-3-(2-ni trophenyl)allyl-idene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)-3-methylpyridin-2-amine
-
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)-4-methylpyridin-2-amine
-
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)-5-(trifluoromethyl)pyridin-2-amine
-
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)pyridin-3-amine
-
(E)-tert-butyl 4-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methyleneamino)piperidine-1-carboxylate
-
1-(2,6-dichlorobenzyl)-5-[(3-methoxybenzyl)oxy]-1H-indole-2-carboxylic acid
-
1-(2,6-dichlorobenzyl)-5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
-
1-(2,6-dichlorobenzyl)-5-[[4-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
an indole derivative, inhibits FabH by 98% at 0.0375 mM
1-(2-bromobenzyl)-5-[(3-methoxybenzyl)oxy]-1H-indole-2-carboxylic acid
-
1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl (2E)-3-(biphenyl-4-yl)prop-2-enoate
-
1-(4-carboxybenzyl)-5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
an indole derivative, inhibits FabH by 80% at 0.040 mM
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
1-(5-carboxypentyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
-
1-(5-carboxypentyl)-5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
-
1-cyclohexyl-N-(2'-hydroxy-1,1':3',1''-terphenyl-5'-yl)-5-oxopyrrolidine-3-carboxamide
-
1-phenylethyl (2Z)-3-[(4,5-dimethyl-2-oxido-1,3,2-dioxaphospholan-2-yl)oxy]but-2-enoate
-
-
1-[(6-chloro-1,3-benzodioxol-5-yl)methyl]-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
1-[3-(4-methoxyphenyl)-5-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
-
1-[4-(trifluoromethyl)benzyl]-5-[[4-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
-
1-[5-(2-chlorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
-
1-[5-(4-bromophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
-
1-[5-(4-chlorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
-
10,10-dimethyl-7-(2-nitrophenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(3-chlorophenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(3-nitrophenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(4-chlorophenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(4-hydroxy-3-methoxyphenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(4-hydroxyphenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(4-nitrophenyl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(naphthalen-2-yl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
10,10-dimethyl-7-(thiophen-2-yl)-10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione
-
-
2,4-dibromo-6-[(E)-(2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene)methyl]phenol
-
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
2,4-dibromo-6-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
2,4-dibromo-6-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
2,4-dichloro-6-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
2,4-dichloro-6-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
2,5-dichloro-4-nitro-N-[4-(trifluoromethyl)phenyl]thiophene-3-sulfonamide
-
-
2-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-5-(2-methylbenzyl)-1,3,4-oxadiazole
-
-
2-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-5-(4-nitrophenyl)-1,3,4-oxadiazol
-
-
2-((4-bromo-3-[(diethylamino)sulfonyl]benzoyl)amino)benzoic acid
benzoylamino-benzoic acid derivative inhibitor-enzyme interaction analysis, overview
2-(2-methoxyphenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
-
-
2-(2-methoxyphenyl)-5-[(2-methyl-5-nitro-1H-imidazol-1-yl)methyl]-1,3,4-oxadiazole
-
2-(2-methyl-5-nitro-1H-imidazol-1-yl)-N'-[(E)-(3,4,5-trimethylphenyl)methylidene]acetohydrazide
-
2-(3-bromophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
-
-
2-(3-diethylsulfamoyl-4-fluorobenzoylamino)benzoic acid
-
IC50 is 0.0084 mM
2-(3-diethylsulfamoyl-4-methoxybenzoylamino)benzoic acid
-
IC50 is 0.0114 mM
2-(3-diethylsulfamoyl-4-phenoxybenzoylamino)benzoic acid
-
IC50 is 0.0061 mM
2-(3-diethylsulfamoyl-4-piperidin-1-ylbenzoylamino)benzoic acid
-
IC50 is 0.0022 mM
2-(3-methoxyphenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
-
-
2-(3-phenoxy-4-piperazin-1-ylbenzoylamino)benzoic acid
-
IC50 is 0.185 mM
2-(3-phenoxy-4-piperidin-1-ylbenzoylamino)benzoic acid
-
IC50 is 0.00029 mM
2-(3-phenoxy-4-pyridin-3-ylbenzoylamino)benzoic acid
-
IC50 is 0.00011 mM
2-(3-phenoxy-4-thiomorpholin-4-ylbenzoylamino)benzoic acid
-
IC50 is 0.0012 mM
2-(3-phenoxybenzoylamino)thiophene-3-carboxylic acid
-
IC50 is 0.043 mM
2-(4-bromo-3-diethylsulfamoyl-5-methylbenzoylamino)-benzoic acid
-
IC50 is 0.16 mM
2-(4-bromo-3-diethylsulfamoylbenzoylamino)-benzoic acid
-
IC50 is 0.0016 mM
2-(4-bromo-3-phenoxybenzoylamino)-6-hydroxybenzoic acid
-
IC50 is 0.000062 mM
2-(4-bromophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
-
-
2-(4-chlorophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
-
-
2-(4-cyclopentylmethoxy-3-diethylsulfamoylbenzoylamino)benzoic acid
-
IC50 is 0.0021 mM
2-(4-fluorophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
-
-
2-(4-morpholin-4-yl-3-phenoxybenzoylamino)benzoic acid
-
IC50 is 0.0032 mM
2-([4-bromo-3-[(diethylamino)sulfonyl]-5-methylbenzoyl]amino)benzoic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)benzoic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)benzoic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
2-([[4-(3,5-dimethylpiperazin-1-yl)-3-phenoxyphenyl]carbonyl]amino)benzoic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
2-([[4-(4-methylpiperazin-1-yl)-3-phenoxyphenyl]carbonyl]amino)benzoic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)benzoic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
2-amino-5-(3-chlorophenyl)thiazole-4-carboxylic acid
MIC value is 0.125 mM
2-amino-5-methylthiazole-4-carboxylic acid
MIC value is 0.00035 mM
2-hydroxy-6-[(2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.000004 mM
2-[(2',4'-difluoro-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00016 mM
2-[(2-diethylsulfamoyl-biphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.0016 mM
2-[(2-phenoxy-3'-trifluoromethoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00047 mM
2-[(2-phenoxy-4'-trifluoromethylbiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.000096 mM
2-[(2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.000056 mM
2-[(2E)-2-[(4-bromophenyl)methylidene]hydrazino]-4-(3,4-dichlorophenyl)-1,3-thiazole
-
-
2-[(2E)-2-[(4-bromophenyl)methylidene]hydrazino]-4-(4-chlorophenyl)-1,3-thiazole
-
-
2-[(2E)-2-[(4-chlorophenyl)methylidene]hydrazino]-4-(3,4-dichlorophenyl)-1,3-thiazole
-
-
2-[(2E)-2-[(4-methoxyphenyl)methylidene]hydrazino]-4-phenyl-1,3-thiazole
-
-
2-[(3',4'-difluoro-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00033 mM
2-[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00057 mM
2-[(3'-isopropyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00079 mM
2-[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00025 mM
2-[(4'-ethoxy-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00022 mM
2-[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00024 mM
2-[(4'-hydroxy-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00041 mM
2-[(4'-methanesulfonyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.000028 mM
2-[(4'-methyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
-
IC50 is 0.00016 mM
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
2-[3-(3,4-dichlorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
2-[3-(4-bromophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-(4-methoxyphenyl)-1,3-thiazole
-
-
2-[3-(4-bromophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
-
2-[3-(4-bromophenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
-
-
2-[3-(4-bromophenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
-
2-[3-(4-fluorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
-
-
2-[3-(4-fluorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
-
2-[3-(4-methoxyphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
-
-
2-[3-(4-methoxyphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
-
2-[3-(4-methylphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
-
-
2-[3-(4-methylphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
-
2-[3-phenoxy-4-(1H-pyrazol-4-yl)benzoylamino]benzoic acid
-
IC50 is 0.022 mM
2-[4-(2,4-dinitrophenyl)-1H-pyrazol-1-yl]-4-(trifluoromethyl)pyrimidine
-
2-[4-(3,5-dimethylpiperazin-1-yl)-3-phenoxybenzoylamino]benzoic acid
-
IC50 is 0.038 mM
2-[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxybenzoylamino]benzoic acid
-
IC50 is 0.00027 mM
2-[4-(4-methylpiperazin-1-yl)-3-phenoxybenzoylamino]benzoic acid
-
IC50 is 0.025 mM
2-[4-[3-bromo-4-(hydroxymethyl)phenyl]piperazin-1-yl]-1-(5-nitrofuran-2-yl)ethanone
-
-
2-[5-(furan-2-yl)-3-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
-
-
2-[5-(furan-2-yl)-3-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-4-(4-methoxyphenyl)-1,3-thiazole
-
-
2-[5-(furan-2-yl)-3-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
-
-
2-[5-(furan-2-yl)-3-phenyl-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
-
-
3-(3-phenoxybenzoylamino)thiophene-2-carboxylic acid
-
IC50 is 0.0101 mM
3-(4-hydroxyphenyl)-1-(2,4,6-tri-hydroxyphenyl)propan-1-one
-
i.e. YKAF04, or 4,2',4',6'-tetrahydroxychalcone, or phloretin
3-bromo-N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]benzamide
fitting 3-bromo-N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]benzamide into the active site of Escherichia coli FabH,PDB ID 3IL9
3-[(1E)-N-(4-methyl-1,3-thiazol-2-yl)ethanehydrazonoyl]phenol
-
i.e. YKA3003
3-[2-(3,4-dihydroxyphenyl)-1-methyl-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
-
i.e. YKA3001
3-[[4-(4-cyclopentylphenoxy)phenyl]methyl]-1,3-thiazolidine-2-thione
-
3-[[4-(4-cyclopentylphenoxy)phenyl]methyl]-1lambda6,3-thiazolidine-1,1,2-trione
-
4'-(2-carboxyphenylcarbamoyl)-2'-phenoxybiphenyl-4-carboxylic acid
-
IC50 is 0.0021 mM
4'-[(3-hydroxy-2,4-dimethyl-5-oxo-2,5-dihydrothiophen-2-yl)methyl]biphenyl-4-carboxylic acid
-
4-(3,4-dichlorophenyl)-2-[(2E)-2-[(4-fluorophenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-(3,4-dichlorophenyl)-2-[(2E)-2-[(4-methoxyphenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-(3,4-dichlorophenyl)-2-[(2E)-2-[(4-methylphenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[(4-chlorophenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[(4-fluorophenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[(4-methoxyphenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[(4-methylphenyl)methylidene]hydrazino]-1,3-thiazole
-
-
4-bromo-2-[(E)-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]phenol
-
4-bromo-2-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
4-bromo-2-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
4-chloro-2-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
4-chloro-2-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
-
-
4-fluoro-2-[(E)-[[2-(4-hydroxyphenyl)ethyl]imino]methyl]phenol
-
4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-one
-
CAS-No. 5338-82-9, IC50 is 0.00078 mM
4-[(1Z)-N,2-bis(4-chlorophenyl)ethanimidoyl]benzene-1,3-diol
-
4-[(2E)-2-[(3-chloro-4-methylphenyl)methylidene]hydrazinyl]benzene-1,3-diol
Ykab-4
4-[(E)-[2-[3-(trifluoromethyl)phenyl]hydrazinylidene]methyl]benzene-1,3-diol
Ykab-6
4-[(E)-[2-[5-(trifluoromethyl)pyridin-2-yl]hydrazinylidene]methyl]benzene-1,3-diol
-
5-chloro-4-phenyl-[1,2]-dithiol-3-one
-
CAS-No. 2425-05-0, IC50 is 0.0019 mM
5-hydroxy-2-phenyl-7-(2-(piperazin-1-yl)ethoxy)-4H-chromen-4-one
a chrysine derivative, strong inhibition with MIC of 0.001560.00625 mg/ml, molecular docking simulation and determination of inhibitor binding structure at the active site, overview
5-hydroxy-2-phenyl-7-(3-(2-hydroxyethylamino)propoxy)-4H-chromen-4-one
-
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
5-hydroxy-7-(2-(4-methylpiperazin-1-yl)ethoxy)-2-phenyl-4H-chromen-4-one
-
5-hydroxy-7-(3-(4-methylpiperazin-1-yl)propoxy)-2-phenyl-4H-chromen-4-one
-
5-[(2,6-dichlorobenzyl)oxy]-1-(4-methoxybenzyl)-1H-indole-2-carboxylic acid
-
5-[(2,6-dichlorobenzyl)oxy]-1-[(6-methyl-1,3-benzodioxol-5-yl)methyl]-1H-indole-2-carboxylic acid
-
5-[(2,6-dichlorobenzyl)oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
an indole derivative, inhibits FabH by 98% at 0.0375 mM
5-[(2-bromobenzyl)oxy]-1-(4-methoxybenzyl)-1H-indole-2-carboxylic acid
-
5-[(2-bromobenzyl)oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
an indole derivative, inhibits FabH by 80% at 0.040 mM
5-[(4-methoxybenzyl)oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
-
5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
-
6-[(2,6-dichlorophenyl)methoxy]-3-(phenylsulfanyl)-1H-indole-2-carboxylic acid
SB418011
7-[4-[(2R)-1-(4-acetylanilino)-1-oxopropan-2-yl]piperazin-1-yl]-1-cyclopropyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
-
acyl-[acyl-carrier protein]
-
mixed inhibition type, the enzyme is a target for fatty acid synthesis regulation by acyl-[acyl-carrier-protein], inhibitory potency increases with increasing chain length between C12 and C20
ampicillin
-
inhibition of the recombinant enzyme in transformed Mycobacterium bovis strain BCG in vivo
butyryl-[acyl-carrier protein]
-
feed-back inhibition of the enzyme via decrease in affinity for acetyl-CoA, inhibition mechanism
decanoyl-[acyl-carrier protein]
-
reversible, noncompetitive inhibition versus malonyl-[acyl-carrier-protein] and uncompetitive versus acetyl-CoA, IC50 is 0.00045 mM
Ethionamide
-
inhibition of the recombinant enzyme in transformed Mycobacterium bovis strain BCG in vivo
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
hexanoyl-[acyl-carrier protein]
-
feed-back inhibition of the enzyme via decrease in affinity for acetyl-CoA, inhibition mechanism
isoniazid
-
inhibition of the recombinant enzyme in transformed Mycobacterium bovis strain BCG in vivo
isoxyl
-
inhibition of the recombinant enzyme in transformed Mycobacterium bovis strain BCG in vivo
methyl 2-(2-bromoacetamido)-5-(3-chlorophenyl) thiazole-4-carboxylate
-
methyl 2-(2-bromoacetamido)-5-phenylthiazole-4-carboxylate
-
methyl 2-amino-5-benzylthiazole-4-carboxylate
MIC value is 240 nM
methyl 2-amino-5-methylthiazole-4-carboxylate
MIC value is 0.093 mM
methyl 5-benzyl-2-(2-bromoacetamido)thiazole-4-carboxylate
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine 2-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(E)-(3,5-dibromo-2,4-dihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
-
N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-hydroxy-3-methoxybenzohydrazide
-
N-(2,4,6-trimethylphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(2-bromo-4-methoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(2-fluoro-4-methoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(3,4,5-trimethoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(3,4-dimethylphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(4-(4-bromophenyl)thiazol-2-yl)-2-(3-chlorophenyl)acetamid
the malonyl carboxylate forms hydrogen bonds to the backbone nitrogen of Phe304, inhibitor binding mode, overview
N-(4-methoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
most potent inhibitor
N-(5-chloropyridin-2-yl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(7-methyl-1H-indazol-3-yl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(naphthalen-1-yl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-(naphthalen-2-yl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-[(4-methoxyphenyl)methyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-[(4-phenoxyphenyl)methyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-[(furan-2-yl)methyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-[2,6-di(propan-2-yl)phenyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-[3,5-bis(trifluoromethyl)phenyl]-4-[[3,5-bis(trifluoromethyl)phenyl]amino]-3-nitrocyclopenta-1,3-diene-1-sulfonamide
-
-
N-[3-[(E)-(5-bromo-2-hydroxybenzylidene)amino]propyl]-2-hydroxybenzamide
-
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-2-(3,4-diethoxyphenyl)acetamide
-
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-2-(3-methoxyphenyl)acetamide
-
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-5,8-dihydronaphthalene-2-carboxamide
-
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]morpholine-4-carboxamide
-
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]naphthalene-1-carboxamide
-
N-[4-(trifluoromethyl)phenyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
N-[[4-(trifluoromethyl)phenyl]methyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
-
naringenin
-
naringenin docks more strongly with efKAS III than apigenin, resulting in the intensive hydrogen bond network between naringenin and efKAS III. Only naringenin shows antibacterial activity against Enterococcus faecalis at 0.256 mg/ml
octanoyl-[acyl-carrier protein]
-
feed-back inhibition of the enzyme via decrease in affinity for acetyl-CoA, inhibition mechanism
rifampicin
-
inhibition of the recombinant enzyme in transformed Mycobacterium bovis strain BCG in vivo
tert-butyl [4-[(3,4-dihydro-2H-1,5-benzodioxepine-7-carbonyl)amino]phenyl]carbamate
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](2-fluorophenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](2-methoxyphenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](2-methylphenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](2-nitrophenyl)methanone
most potent inhibitor
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](3-fluorophenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](3-methoxyphenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](3-methylphenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](3-nitrophenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](4-fluorophenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](4-methoxyphenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](4-methylphenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](4-nitrophenyl)methanone
-
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](phenyl)methanone
-
(E) -N'-((E)-3-(2-Ni trophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E) -N'-((E)-3-(2-Ni trophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
-
(E)-N'-((E)-3-(2-methoxyphenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-(2-methoxyphenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-(2-nitrophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-(2-nitrophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-(4-bromophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-(4-bromophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-(4-bromophenyl)allylidene)-2,3-dihydrobenzo[b][1,4]dioxine-2-carbohydrazide
-
-
(E)-N'-((E)-3-phenylallylidene)-2,3-dihydrobenzo[b][1,4]-dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-phenylallylidene)-2,3-dihydrobenzo[b][1,4]-dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-phenylallylidene)-2,3-dihydrobenzo[b][1,4]-dioxine-2-carbohydrazide
-
(E)-N'-((E)-3-phenylallylidene)-2,3-dihydrobenzo[b][1,4]-dioxine-2-carbohydrazide
-
-
1-(4-carboxybutyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
-
-
1-(4-carboxybutyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
-
-
1-[(6-chloro-1,3-benzodioxol-5-yl)methyl]-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
-
-
1-[(6-chloro-1,3-benzodioxol-5-yl)methyl]-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
-
-
1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
-
1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
-
2,5-anhydro-3,4-dideoxy-3-[[(3-phenoxyphenyl)carbonyl]amino]-2-thiopentonic acid
-
-
2,5-anhydro-3,4-dideoxy-3-[[(3-phenoxyphenyl)carbonyl]amino]-2-thiopentonic acid
-
-
2,5-anhydro-3,4-dideoxy-3-[[(3-phenoxyphenyl)carbonyl]amino]-2-thiopentonic acid
-
-
2,5-anhydro-3,4-dideoxy-3-[[(3-phenoxyphenyl)carbonyl]amino]-2-thiopentonic acid
-
-
2,5-anhydro-3,4-dideoxy-3-[[(3-phenoxyphenyl)carbonyl]amino]-2-thiopentonic acid
-
-
2,5-anhydro-3,4-dideoxy-3-[[(3-phenoxyphenyl)carbonyl]amino]-2-thiopentonic acid
-
-
2-([[2-(diethylsulfamoyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-(diethylsulfamoyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-(diethylsulfamoyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-(diethylsulfamoyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-(diethylsulfamoyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-(diethylsulfamoyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-3'-(trifluoromethoxy)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[2-phenoxy-4'-(trifluoromethyl)biphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3'-(1-methylethyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3'-(1-methylethyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3'-(1-methylethyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3'-(1-methylethyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3'-(1-methylethyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3'-(1-methylethyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(4-fluorophenoxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(4-fluorophenoxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(4-fluorophenoxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(4-fluorophenoxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(4-fluorophenoxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(4-fluorophenoxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-fluorophenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-fluorophenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-fluorophenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-fluorophenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-fluorophenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-fluorophenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-methoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-methoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-methoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-methoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-methoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-methoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(diethylsulfamoyl)-4-piperidin-1-ylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(pyridin-2-yloxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(pyridin-2-yloxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(pyridin-2-yloxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(pyridin-2-yloxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(pyridin-2-yloxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-(pyridin-2-yloxy)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-phenoxy-4-(1H-pyrazol-4-yl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-phenoxy-4-(1H-pyrazol-4-yl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-phenoxy-4-(1H-pyrazol-4-yl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-phenoxy-4-(1H-pyrazol-4-yl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-phenoxy-4-(1H-pyrazol-4-yl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[3-phenoxy-4-(1H-pyrazol-4-yl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4'-(methylsulfonyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4'-(methylsulfonyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4'-(methylsulfonyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4'-(methylsulfonyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4'-(methylsulfonyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4'-(methylsulfonyl)-2-phenoxybiphenyl-4-yl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)benzoic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)benzoic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-(cyclopentylmethoxy)-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)-5-methylphenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-([[4-bromo-3-(diethylsulfamoyl)phenyl]carbonyl]amino)cyclohexanecarboxylic acid
-
-
2-hydroxy-6-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
-
-
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(3,5-dimethylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[([4-[(4-methylpiperazin-1-yl)methyl]-3-phenoxyphenyl]carbonyl)amino]cyclohexanecarboxylic acid
-
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-hydroxy-6-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-hydroxy-6-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-hydroxy-6-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-hydroxy-6-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-hydroxy-6-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-hydroxy-6-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3',4'-difluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperazin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperazin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperazin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperazin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperazin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperazin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperidin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperidin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperidin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperidin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperidin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-piperidin-1-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-pyridin-3-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-pyridin-3-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-pyridin-3-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-pyridin-3-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-pyridin-3-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-pyridin-3-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]benzoic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]piperidine-3-carboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]tetrahydrothiophene-3-carboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]tetrahydrothiophene-3-carboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]tetrahydrothiophene-3-carboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]tetrahydrothiophene-3-carboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]tetrahydrothiophene-3-carboxylic acid
-
-
2-[[(3-phenoxyphenyl)carbonyl]amino]tetrahydrothiophene-3-carboxylic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-ethoxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-ethoxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-ethoxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-ethoxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-ethoxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-ethoxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]-6-hydroxybenzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]-6-hydroxybenzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]-6-hydroxybenzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]-6-hydroxybenzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]-6-hydroxybenzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]-6-hydroxybenzoic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-hydroxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-hydroxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-hydroxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-hydroxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-hydroxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-hydroxy-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4'-methyl-2-phenoxybiphenyl-4-yl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-hydroxy-5-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-hydroxy-5-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-hydroxy-5-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-hydroxy-5-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-hydroxy-5-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-hydroxy-5-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-bromo-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-fluoro-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-fluoro-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-fluoro-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-fluoro-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-fluoro-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-hydroxy-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-hydroxy-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-hydroxy-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-hydroxy-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-hydroxy-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-hydroxy-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-morpholin-4-yl-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-morpholin-4-yl-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-morpholin-4-yl-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-morpholin-4-yl-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-morpholin-4-yl-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
2-[[(4-morpholin-4-yl-3-phenoxyphenyl)carbonyl]amino]cyclohexanecarboxylic acid
-
-
3-(biphenyl-4-ylmethyl)-1,3-thiazolidin-2-one 1,1-dioxide
IC50: 0.0009 mM
3-(biphenyl-4-ylmethyl)-1,3-thiazolidin-2-one 1,1-dioxide
-
IC50: 0.0494 mM
3-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2-thione
IC50: 0.0177 mM; IC50: 0.1 mM, above
3-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2-thione
-
IC50: 0.0053 mM; IC50: 0.0556 mM
3-[(4'-cyclopentylbiphenyl-4-yl)methyl]-1,3-thiazolidin-2-one 1,1-dioxide
IC50: 0.0024 mM
3-[(4'-cyclopentylbiphenyl-4-yl)methyl]-1,3-thiazolidin-2-one 1,1-dioxide
-
IC50: 0.0108 mM
3-[4-(4-cyclopentylphenoxy)benzyl]-1,3-thiazolidin-2-one 1,1-dioxide
-
3-[4-(4-cyclopentylphenoxy)benzyl]-1,3-thiazolidin-2-one 1,1-dioxide
-
-
3-[[(3-phenoxyphenyl)carbonyl]amino]piperidine-2-carboxylic acid
-
-
4'-[(2-carboxycyclohexyl)carbamoyl]-2'-phenoxybiphenyl-4-carboxylic acid
-
-
4'-[(2-carboxycyclohexyl)carbamoyl]-2'-phenoxybiphenyl-4-carboxylic acid
-
-
4'-[(2-carboxycyclohexyl)carbamoyl]-2'-phenoxybiphenyl-4-carboxylic acid
-
-
4'-[(2-carboxycyclohexyl)carbamoyl]-2'-phenoxybiphenyl-4-carboxylic acid
-
-
4'-[(2-carboxycyclohexyl)carbamoyl]-2'-phenoxybiphenyl-4-carboxylic acid
-
-
4'-[(2-carboxycyclohexyl)carbamoyl]-2'-phenoxybiphenyl-4-carboxylic acid
-
-
4-(4-biphenyl-4-ylcyclohexyl)-1,3-thiazolidine-2-thione
IC50: 0.0177 mM
4-(4-biphenyl-4-ylcyclohexyl)-1,3-thiazolidine-2-thione
-
IC50: 0.0053 mM
5-chloro-1,2-dithiole-3-ones
binding mode, structural features for optimal complex formation, inhibition potencies of derivatives, the derivatives differ in case of reversibility of the inhibition dependent on the substituting groups, overview
5-chloro-1,2-dithiole-3-ones
-
binding mode, structural features for optimal complex formation, inhibition potencies of derivatives, the derivatives differ in case of reversibility of the inhibition dependent on the substituting groups, overview
5-chloro-1,2-dithiole-3-thiones
binding mode, structural features for optimal complex formation, inhibition potencies of derivatives, the derivatives differ in case of reversibility of the inhibition dependent on the substituting groups, overview
5-chloro-1,2-dithiole-3-thiones
-
binding mode, structural features for optimal complex formation, inhibition potencies of derivatives, the derivatives differ in case of reversibility of the inhibition dependent on the substituting groups, overview
methyl-CoA disulfide
inhibition mechanism involving enzyme residues His249 and Cys112, overview
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
-
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
N'-[(1E,2E)-3-phenylprop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
-
-
penicillin G
fitting penicillin G into the active site of Escherichia coli FabH, PDB ID 3IL9
thiolactomycin
-
inhibition of the purified enzyme in vitro, and of the recombinant enzyme in transformed Mycobacterium bovis strain BCG in vivo
additional information
synthesis and evaluation of three series of 21 cinnamaldehyde acylhydrazone derivatives for FabH-inhibitory activity, active site docking simulation and binding model, based on the Escherichia ccoli FabH-CoA complex structure, PDB ID 1HNJ. Antibacterial activity of the synthesized 1,4-benzodioxan derivatives compounds, MIC values, overview
-
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
-
additional information
-
inhibitor design by computational chemistry, antibacterial potency of inhibitors, overview
-
additional information
-
HQSAR study of beta-ketoacyl-acyl-carrier protein synthase III (FabH) inhibitors
-
additional information
-
benzoylaminobenzoic acid derivatives: inhibitor design and quantitative structure-activity relationship studies, the compounds show FabH inhibitory activity in cell free and whole cell system, overview. The inhibitory activity increases with increase in hydrophobicity, molar refractivity, aromaticity, and presence of OH group, on x position of the nucleus. The presence of hetero-atoms like N, O, or S at R1 position of the nucleus decreases the inhibitory activity
-
additional information
-
no inhibition by non-esterified [acyl-carrier-protein]
-
additional information
-
no significant inhibitory activity at 0.3 mM: butyl-CoA disulfide, sec-butyl-CoA disulfide, octyl-CoA disulfide, decyl-CoA disulfide
-
additional information
-
inhibitor design and synthesis, analysis of inhibitory potencies against FabH and antibacterial activities, overview
-
additional information
-
benzoylaminobenzoic acid derivatives: inhibitor design and quantitative structure-activity relationship studies, the compounds show FabH inhibitory activity in cell free and whole cell system, overview. The inhibitory activity increases with increase in hydrophobicity, molar refractivity, aromaticity, and presence of OH group, on x position of the nucleus. The presence of hetero-atoms like N, O, or S at R1 position of the nucleus decreases the inhibitory activity
-
additional information
design, synthesis and antibacterial activity studies of thiazole derivatives as potent ecKAS III inhibitors, inhibitor antibacterial activity against the respective Gram-negative and Gram-positive bacterial strains, overview
-
additional information
-
design, synthesis and antibacterial activity studies of thiazole derivatives as potent ecKAS III inhibitors, inhibitor antibacterial activity against the respective Gram-negative and Gram-positive bacterial strains, overview
-
additional information
synthesis and evaluation of three series of 21 cinnamaldehyde acylhydrazone derivatives for FabH-inhibitory activity, active site docking simulation and binding model, based on the Escherichia coli FabH-CoA complex structure, PDB ID 1HNJ. Antibacterial activity of the synthesized 1,4-benzodioxan derivatives compounds, MIC values, overview
-
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
-
additional information
design and synthesis of thiazole derivatives as potent FabH inhibitors with antibacterial activity, MIC values, docking simulation and structure-activity relationsship study, binding mode, overview
-
additional information
the dimer interface could be a potential target for anti-infection drug discovery, structure-based inhibitor design, overview. Cerulenin is no inhibitor of FabH
-
additional information
indole analogue inhibitor-enzyme interaction analysis, overview
-
additional information
2-tosylnaphthalene-1,4-diol analogues are reversible inhibitors (10-20 nM) of Escherichia coli FabH. The sulfonyl group and naphthalene-1,4 diol are required for activity against all enzymes but the toluene portion can be significantly altered. Inhibitors are also effective against the Mycobacterium tuberculosis (EC 2.3.1.301) and Plasmodium falciparum FabH enzymes; synthesis and evalutation of cyclic sulfones. The compounds are selectively active against Escherichia coli FabH, but not Mycobacterium tuberculosis FabH (EC 2.3.1.301) or Plasmodium falciparum KASIII
-
additional information
-
inhibitor design, structures, and binding analysis, antibacterial activities, overview
-
additional information
-
inhibitor structure analysis by NMR, binding analysis, and antibacterial activities, overview
-
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
-
additional information
-
the mitochondrial enzyme is not affected by cerulenin
-
additional information
no enzyme inhibition by several derivatives of cyclic sulfones, overview
-
additional information
-
no enzyme inhibition by several derivatives of cyclic sulfones, overview
-
additional information
-
no significant inhibitory activity at 0.3 mM: methyl-CoA disulfide, butyl-CoA disulfide, sec-butyl-CoA disulfide
-
additional information
modeling studies of binding of 2-aminothiazole-4-carboxylate analogues to FabH, overview
-
additional information
-
modeling studies of binding of 2-aminothiazole-4-carboxylate analogues to FabH, overview
-
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
-
additional information
-
benzoylaminobenzoic acid derivatives: inhibitor design and quantitative structure-activity relationship studies, the compounds show FabH inhibitory activity in cell free and whole cell system, overview. The inhibitory activity increases with increase in hydrophobicity, molar refractivity, aromaticity, and presence of OH group, on x position of the nucleus. The presence of hetero-atoms like N, O, or S at R1 position of the nucleus decreases the inhibitory activity
-
additional information
-
2-tosylnaphthalene-1,4-diol analogues are reversible inhibitors of Plasmodium falciparum FabH. The sulfonyl group and naphthalene-1,4 diol are required for activity against all enzymes but the toluene portion can be significantly altered. Inhibitors are also effective against the Mycobacterium tuberculosis (EC 2.3.1.301) and Escherichia coli FabH enzymes
-
additional information
synthesis and evaluation of three series of 21 cinnamaldehyde acylhydrazone derivatives for FabH-inhibitory activity, active site docking simulation and binding model, based on the Escherichia ccoli FabH-CoA complex structure, PDB ID 1HNJ. Antibacterial activity of the synthesized 1,4-benzodioxan derivatives compounds, MIC values, overview
-
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
-
additional information
-
antibacterial potency of inhibitors, overview
-
additional information
-
benzoylaminobenzoic acid derivatives: inhibitor design and quantitative structure-activity relationship studies, the compounds show FabH inhibitory activity in cell free and whole cell system, overview. The inhibitory activity increases with increase in hydrophobicity, molar refractivity, aromaticity, and presence of OH group, on x position of the nucleus. The presence of hetero-atoms like N, O, or S at R1 position of the nucleus decreases the inhibitory activity
-
additional information
-
synthesis and evaluation of three series of 21 cinnamaldehyde acylhydrazone derivatives for FabH-inhibitory activity, active site docking simulation and binding model, based on the Escherichia ccoli FabH-CoA complex structure, PDB ID 1HNJ. Antibacterial activity of the synthesized 1,4-benzodioxan derivatives compounds, MIC values, overview
-
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
-
additional information
-
benzoylaminobenzoic acid derivatives: inhibitor design and quantitative structure-activity relationship studies, the compounds show FabH inhibitory activity in cell free and whole cell system, overview. The inhibitory activity increases with increase in hydrophobicity, molar refractivity, aromaticity, and presence of OH group, on x position of the nucleus. The presence of hetero-atoms like N, O, or S at R1 position of the nucleus decreases the inhibitory activity
-
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
-
additional information
-
benzoylaminobenzoic acid derivatives: inhibitor design and quantitative structure-activity relationship studies, the compounds show FabH inhibitory activity in cell free and whole cell system, overview. The inhibitory activity increases with increase in hydrophobicity, molar refractivity, aromaticity, and presence of OH group, on x position of the nucleus. The presence of hetero-atoms like N, O, or S at R1 position of the nucleus decreases the inhibitory activity
-
additional information
inhibitor interaction with the active site, structure analysis, docking study, overview. Cerulenin is a poor inhibitor of FabH
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the acpP gene product stimulates fatty acid biosynthesis in vitro
-
additional information
-
the acpP gene product stimulates fatty acid biosynthesis in vitro
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anthrax
Unsymmetric aryl-alkyl disulfide growth inhibitors of methicillin-resistant Staphylococcus aureus and Bacillus anthracis.
Infections
Unsymmetric aryl-alkyl disulfide growth inhibitors of methicillin-resistant Staphylococcus aureus and Bacillus anthracis.
Tuberculosis
3D-QSAR, molecular docking studies, and binding mode prediction of thiolactomycin analogs as mtFabH inhibitors.
Tuberculosis
Acetylene-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme.
Tuberculosis
Biphenyl-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme.
Tuberculosis
Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A.
Tuberculosis
Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III.
Tuberculosis
Identification and substrate specificity of beta -ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis.
Tuberculosis
Identification of 2-Aminothiazole-4-Carboxylate Derivatives Active against Mycobacterium tuberculosis H(37)R(v) and the beta-Ketoacyl-ACP Synthase mtFabH.
Tuberculosis
Mycobacterium tuberculosis beta-ketoacyl acyl carrier protein synthase III (mtFabH) assay: principles and method.
Tuberculosis
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates.
Tuberculosis
Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity.
Tuberculosis
Synthesis and biological evaluation of thiazolidine-2-one 1,1-dioxide as inhibitors of Escherichia coli beta-ketoacyl-ACP-synthase III (FabH).
Tuberculosis
The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
acetyl-CoA
-
pH 7.0, 25°C, recombinant enzyme from Brassica napus seeds
0.0037
malonyl-[acyl-carrier protein]
-
pH 7.0, 30°C, recombinant His-tagged enzyme
0.0186
malonyl-[acyl-carrier protein]
pH 7.0, recombinant enzyme
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
6-methylsalicyl-N-acetylcysteamine
at pH 7.5 and 25°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02215
(3-chlorophenyl)[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl]methanone
Escherichia coli
pH and temperature not specified in the publication
0.08
(5R)-4-hydroxy-3,5-dimethyl-5-tetradecylthiophen-2(5H)-one
Mycobacterium tuberculosis
-
-
0.017 - 0.019
(5R)-4-hydroxy-5-[[4'-(hydroxymethyl)biphenyl-4-yl]methyl]-3,5-dimethylthiophen-2(5H)-one
0.00702
(5R)-5-[3-(4-acetyl-3-hydroxyphenyl)prop-2-yn-1-yl]-4-hydroxy-3,5-dimethylthiophen-2(5H)-one
Mycobacterium tuberculosis
-
-
0.00404
(5R)-5-[3-(4-acetylphenyl)prop-2-yn-1-yl]-4-hydroxy-3,5-dimethylthiophen-2(5H)-one
Mycobacterium tuberculosis
-
-
0.0094
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(2,4-dichlorophenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0401
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(2-bromophenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0275
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(3-bromophenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0082
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(3-fluorophenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0067
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-(benzyloxy)phenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0198
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-(dimethylamino)phenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0156
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-bromophenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0343
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(4-chlorophenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0025
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(biphenyl-4-yl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0489
(E)-1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl 3-(naphthalen-1-yl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0067
(E)-1-(6-chloropyridin-3-yl)-N-((3,4-dihydro-2Hbenzo[b][1,4]dioxepin-7-yl)methylene)methanamine
Escherichia coli
at pH 7.0 and 37°C
0.0123
(E)-4-chloro-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methylene)pyridin-2-amine
Escherichia coli
at pH 7.0 and 37°C
0.0128
(E)-5-chloro-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methylene)pyridin-2-amine
Escherichia coli
at pH 7.0 and 37°C
0.0099
(E)-6-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methyleneamino)nicotinonitrile
Escherichia coli
at pH 7.0 and 37°C
0.043
(E)-ethyl 2-(4-(benzyloxy)phenyl)-3-(4-bromophenylamino)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0085
(E)-ethyl 2-(4-(benzyloxy)phenyl)-3-(4-isopropylphenylamino)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0857
(E)-N'-((E)-3-phenylallylidene)-2,3-dihydrobenzo[b][1,4]-dioxine-2-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0074
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)-3-methylpyridin-2-amine
Escherichia coli
at pH 7.0 and 37°C
0.0151
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)-4-methylpyridin-2-amine
Escherichia coli
at pH 7.0 and 37°C
0.0038
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)-5-(trifluoromethyl)pyridin-2-amine
Escherichia coli
at pH 7.0 and 37°C
0.0145
(E)-N-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)-methylene)pyridin-3-amine
Escherichia coli
at pH 7.0 and 37°C
0.0021
(E)-tert-butyl 4-((3,4-dihydro-2H-benzo[b][1,4]dioxepin-7-yl)methyleneamino)piperidine-1-carboxylate
Escherichia coli
at pH 7.0 and 37°C
0.024
(Z)-ethyl 2-(4-(benzyloxy)phenyl)-3-(2,4-dibromophenylamino)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.028
(Z)-ethyl 2-(4-(benzyloxy)phenyl)-3-(2-chlorophenylamino)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0033
(Z)-ethyl 2-(4-(benzyloxy)phenyl)-3-(4-bromophenylamino)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0082
(Z)-ethyl 2-(4-(benzyloxy)phenyl)-3-(4-fluorophenylamino)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0026
(Z)-ethyl 3-(p-toluidino)-2-(4-(benzyloxy)phenyl)acrylate
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.015
1-(2,6-dichlorobenzyl)-5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.004
1-(2,6-dichlorobenzyl)-5-[[4-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.017
1-(2-bromobenzyl)-5-[(3-methoxybenzyl)oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.0515
1-(2-chlorophenyl)-1-(3,5-dibromo-2-hydroxybenzyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0025
1-(2-methyl-5-nitro-1H-imidazol-1-yl)propan-2-yl (2E)-3-(biphenyl-4-yl)prop-2-enoate
Escherichia coli
pH and temperature not specified in the publication
0.0717
1-(3,5-dibromo-2-hydroxybenzyl)-1-(4-fluorophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.04
1-(4-carboxybenzyl)-5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.00014 - 0.007
1-(4-carboxybutyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
0.0101
1-(4-chlorophenyl)-1-(3,5-dibromo-2-hydroxybenzyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0043
1-(4-[(E)-[3-(benzyloxy)benzylidene]amino]phenyl)-3-phenylthiourea
Escherichia coli
pH and temperature not specified in the publication
0.0564
1-(5-bromo-2-hydroxybenzyl)-1-(2-bromophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0218
1-(5-bromo-2-hydroxybenzyl)-1-(2-chlorophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0374
1-(5-bromo-2-hydroxybenzyl)-1-(2-fluorophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.041
1-(5-bromo-2-hydroxybenzyl)-1-(4-bromophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0066
1-(5-bromo-2-hydroxybenzyl)-1-(4-fluorophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.042
1-(5-carboxypentyl)-5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.0258
1-phenylethyl (2Z)-3-[(4,5-dimethyl-2-oxido-1,3,2-dioxaphospholan-2-yl)oxy]but-2-enoate
Plasmodium falciparum
-
-
0.00004 - 0.00088
1-[(6-chloro-1,3-benzodioxol-5-yl)methyl]-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
0.0196
1-[3,5-bis(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0173
1-[3-(4-methoxyphenyl)-5-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0467
1-[3-(4-methoxyphenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.007 - 0.036
1-[4-(trifluoromethyl)benzyl]-5-[[4-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
0.0314
1-[5-(2-chlorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0104
1-[5-(4-bromophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0076
1-[5-(4-chlorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0036
2,4-dibromo-6-[(E)-[2-[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]phenol
Escherichia coli
pH and temperature not specified in the publication
0.0036
2,4-dibromo-6-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0784
2,4-dibromo-6-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0165
2,4-dichloro-6-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0576
2,4-dichloro-6-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.00028
2,5-dichloro-4-nitro-N-[4-(trifluoromethyl)phenyl]thiophene-3-sulfonamide
Plasmodium falciparum
-
-
0.0022
2,5-dichloro-N-[4-(trifluoromethyl)phenyl]thiophene-3-sulfonamide
Plasmodium falciparum
-
-
0.0051
2-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-5-(2-methylbenzyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0405
2-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-5-(4-nitrophenyl)-1,3,4-oxadiazol
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0016
2-((4-bromo-3-[(diethylamino)sulfonyl]benzoyl)amino)benzoic acid
Enterococcus faecalis
pH and temperature not specified in the publication
0.0043
2-(2-methoxyphenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0043
2-(2-methoxyphenyl)-5-[(2-methyl-5-nitro-1H-imidazol-1-yl)methyl]-1,3,4-oxadiazole
Escherichia coli
pH and temperature not specified in the publication
0.0169
2-(3-bromophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0269
2-(3-bromophenyl)-N-(4-phenyl-1,3-thiazol-2-yl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0098
2-(3-bromophenyl)-N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0123
2-(3-chlorophenyl)-N-(4-phenyl-1,3-thiazol-2-yl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0084
2-(3-diethylsulfamoyl-4-fluorobenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0084 mM
0.0114
2-(3-diethylsulfamoyl-4-methoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0114 mM
0.0061
2-(3-diethylsulfamoyl-4-phenoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0061 mM
0.0022
2-(3-diethylsulfamoyl-4-piperidin-1-ylbenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0022 mM
0.0094
2-(3-methoxyphenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.185
2-(3-phenoxy-4-piperazin-1-ylbenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.185 mM
0.00029
2-(3-phenoxy-4-piperidin-1-ylbenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.00029 mM
0.00011
2-(3-phenoxy-4-pyridin-3-ylbenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.00011 mM
0.0012
2-(3-phenoxy-4-thiomorpholin-4-ylbenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0012 mM
0.043
2-(3-phenoxybenzoylamino)thiophene-3-carboxylic acid
Enterococcus faecalis
-
IC50 is 0.043 mM
0.16
2-(4-bromo-3-diethylsulfamoyl-5-methylbenzoylamino)-benzoic acid
Enterococcus faecalis
-
IC50 is 0.16 mM
0.0016
2-(4-bromo-3-diethylsulfamoylbenzoylamino)-benzoic acid
Enterococcus faecalis
-
IC50 is 0.0016 mM
0.000062
2-(4-bromo-3-phenoxybenzoylamino)-6-hydroxybenzoic acid
Enterococcus faecalis
-
IC50 is 0.000062 mM
0.0011
2-(4-bromo-3-phenoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0011 mM
0.0438
2-(4-bromophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0481
2-(4-bromophenyl)-N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0283
2-(4-chlorophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0418
2-(4-chlorophenyl)-N-(4-phenyl-1,3-thiazol-2-yl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0021
2-(4-cyclopentylmethoxy-3-diethylsulfamoylbenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0021 mM
0.0038
2-(4-fluoro-3-phenoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0038 mM
0.0186
2-(4-fluorophenyl)-5-((2-methyl-5-nitro-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0384
2-(4-fluorophenyl)-N-(4-phenyl-1,3-thiazol-2-yl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0001872
2-(4-methylbenzene-1-sulfonyl)naphthalene-1,4-dione
Escherichia coli
pH 7.4, 23°C
0.0032
2-(4-morpholin-4-yl-3-phenoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.0032 mM
0.0057
2-([[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxyphenyl]carbonyl]amino)benzoic acid
Escherichia coli
-
-
0.006
2-fluoro-6-(3-phenoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.006 mM
0.00041
2-hydroxy-6-(3-phenoxybenzoylamino)benzoic acid
Enterococcus faecalis
-
IC50 is 0.00041 mM
0.000004
2-hydroxy-6-[(2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.000004 mM
0.00016
2-[(2',4'-difluoro-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00016 mM
0.0016
2-[(2-diethylsulfamoyl-biphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.0016 mM
0.00047
2-[(2-phenoxy-3'-trifluoromethoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00047 mM
0.000096
2-[(2-phenoxy-4'-trifluoromethylbiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.000096 mM
0.000056
2-[(2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.000056 mM
0.00033
2-[(3',4'-difluoro-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00033 mM
0.00057
2-[(3'-chloro-4'-fluoro-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00057 mM
0.00079
2-[(3'-isopropyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00079 mM
0.00025
2-[(4'-chloro-3'-methyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00025 mM
0.00022
2-[(4'-ethoxy-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00022 mM
0.00024
2-[(4'-fluoro-3'-methyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00024 mM
0.00041
2-[(4'-hydroxy-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00041 mM
0.000028
2-[(4'-methanesulfonyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.000028 mM
0.00016
2-[(4'-methyl-2-phenoxybiphenyl-4-carbonyl)amino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00016 mM
0.0046
2-[3-(3,4-dichlorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
pH and temperature not specified in the publication
0.0037
2-[3-(3-carboxyphenoxy)benzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.0037 mM
0.0197
2-[3-(4-bromophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-(4-methoxyphenyl)-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0097
2-[3-(4-bromophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0271
2-[3-(4-bromophenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0233
2-[3-(4-bromophenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0044
2-[3-(4-carboxyphenoxy)benzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.0044 mM
0.005
2-[3-(4-fluorophenoxy)benzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.005 mM
0.0084
2-[3-(4-fluorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0223
2-[3-(4-fluorophenyl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0899
2-[3-(4-methoxyphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0306
2-[3-(4-methoxyphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0136
2-[3-(4-methylphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0109
2-[3-(4-methylphenyl)-5-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.01
2-[3-(pyridin-4-yloxy)benzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.010 mM
0.022
2-[3-phenoxy-4-(1H-pyrazol-4-yl)benzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.022 mM
0.038
2-[4-(3,5-dimethylpiperazin-1-yl)-3-phenoxybenzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.038 mM
0.00027
2-[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxybenzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.00027 mM
0.025
2-[4-(4-methylpiperazin-1-yl)-3-phenoxybenzoylamino]benzoic acid
Enterococcus faecalis
-
IC50 is 0.025 mM
0.0032
2-[4-[3-bromo-4-(hydroxymethyl)phenyl]piperazin-1-yl]-1-(5-nitrofuran-2-yl)ethanone
Plasmodium falciparum
-
-
0.0184
2-[5-(furan-2-yl)-3-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4(5H)-one
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0157
2-[5-(furan-2-yl)-3-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-4-(4-methoxyphenyl)-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0046
2-[5-(furan-2-yl)-3-(4-methylphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-4-phenyl-1,3-thiazole
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.001
2-[[(3-phenoxy-4-thiomorpholin-4-ylphenyl)carbonyl]amino]benzoic acid
Escherichia coli
-
-
0.0019
3-(2-phenylethyl)-1lambda6,3-thiazolidine-1,1,2-trione
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.29
3-(3-phenoxybenzoylamino)pyridine-2-carboxylic acid
Enterococcus faecalis
-
IC50 is 0.290 mM
0.0101
3-(3-phenoxybenzoylamino)thiophene-2-carboxylic acid
Enterococcus faecalis
-
IC50 is 0.0101 mM
0.0011
3-benzyl-1lambda6,3-thiazolidine-1,1,2-trione
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0269
3-bromo-N-(4-phenyl-1,3-thiazol-2-yl)benzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0058
3-bromo-N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]benzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0123
3-chloro-N-(4-phenyl-1,3-thiazol-2-yl)benzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0109
3-[(4-phenoxyphenyl)methyl]-1,3-thiazolidin-2-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0009
3-[(4-phenoxyphenyl)methyl]-1lambda6,3-thiazolidine-1,1,2-trione
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0144
3-[[4-(4-cyclopentylphenoxy)phenyl]methyl]-1,3-thiazolidin-2-one
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0177
3-[[4-(4-cyclopentylphenoxy)phenyl]methyl]-1,3-thiazolidine-2-thione
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0024
3-[[4-(4-cyclopentylphenoxy)phenyl]methyl]-1lambda6,3-thiazolidine-1,1,2-trione
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.0021
4'-(2-carboxyphenylcarbamoyl)-2'-phenoxybiphenyl-4-carboxylic acid
Enterococcus faecalis
-
IC50 is 0.0021 mM
0.003
4'-[(3-hydroxy-2,4-dimethyl-5-oxo-2,5-dihydrothiophen-2-yl)methyl]biphenyl-4-carboxylic acid
Mycobacterium tuberculosis
-
0.0434
4-bromo-2-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0068
4-bromo-2-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0481
4-bromo-N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]benzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0396
4-chloro-2-[(E)-[[4-(3,4-dichlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0117
4-chloro-2-[(E)-[[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazono]methyl]phenol
Escherichia coli
-
-
0.0418
4-chloro-N-(4-phenyl-1,3-thiazol-2-yl)benzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0027
4-fluoro-2-[(E)-[[2-(4-hydroxyphenyl)ethyl]imino]methyl]phenol
Escherichia coli
pH and temperature not specified in the publication
0.0384
4-fluoro-N-(4-phenyl-1,3-thiazol-2-yl)benzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.00078
4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-one
Staphylococcus aureus
-
CAS-No. 5338-82-9, IC50 is 0.00078 mM
0.0018
4-[(1Z)-N,2-bis(4-chlorophenyl)ethanimidoyl]benzene-1,3-diol
Escherichia coli
pH and temperature not specified in the publication
0.718
5-benzyl-2-(2-bromoacetamido)thiazole-4-carboxylic acid
Mycobacterium tuberculosis
-
0.0019
5-chloro-4-phenyl-[1,2]-dithiol-3-one
Staphylococcus aureus
-
CAS-No. 2425-05-0, IC50 is 0.0019 mM
0.017
5-[(2,6-dichlorobenzyl)oxy]-1-(4-methoxybenzyl)-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.006
5-[(2,6-dichlorobenzyl)oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.017
5-[(2-bromobenzyl)oxy]-1-(4-methoxybenzyl)-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.002
5-[(2-bromobenzyl)oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.02
5-[(4-methoxybenzyl)oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.015
5-[[2-fluoro-6-(trifluoromethyl)benzyl]oxy]-1-[4-(trifluoromethyl)benzyl]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.00045
decanoyl-[acyl-carrier protein]
Cuphea lanceolata
-
reversible, noncompetitive inhibition versus malonyl-[acyl-carrier-protein] and uncompetitive versus acetyl-CoA, IC50 is 0.00045 mM
0.0026
ethyl (2Z)-2-[4-(benzyloxy)phenyl]-3-[(4-methylphenyl)amino]prop-2-enoate
Escherichia coli
pH and temperature not specified in the publication
0.00243
methyl 2-(2-bromoacetamido)-5-(3-chlorophenyl) thiazole-4-carboxylate
Mycobacterium tuberculosis
-
0.0032
methyl 2-(2-bromoacetamido)-5-phenylthiazole-4-carboxylate
Mycobacterium tuberculosis
-
0.1598
methyl 5-benzyl-2-(2-bromoacetamido)thiazole-4-carboxylate
Mycobacterium tuberculosis
-
0.1
N'-[(1E,2E)-3-(2-fluorophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
Escherichia coli
above, pH 7.4, 37°C
0.0035
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0147
N'-[(1E,2E)-3-(2-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0113
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0148
N'-[(1E,2E)-3-(4-bromophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0591
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0066
N'-[(1E,2E)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-6-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.009
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-2-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0094
N'-[(1E,2E)-3-(4-nitrophenyl)prop-2-en-1-ylidene]-2,3-dihydro-1,4-benzodioxine-5-carbohydrazide
Escherichia coli
pH 7.4, 37°C
0.0021
N'-[(E)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-4-hydroxy-3-methoxybenzohydrazide
Escherichia coli
pH and temperature not specified in the publication
0.0271
N-(2-bromo-4-methoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0038
N-(2-fluoro-4-methoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0077
N-(2-fluorophenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0086
N-(3,4,5-trimethoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0326
N-(3,4-dimethylphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.00088
N-(3-(5-bromo-2-hydroxybenzylideneamino)propyl)-2-hydroxybenzamide
Escherichia coli
pH and temperature not specified in the publication
0.0085
N-(3-fluorophenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0053
N-(4-(4-bromophenyl)thiazol-2-yl)-2-(3-chlorophenyl)acetamid
Escherichia coli
pH and temperature not specified in the publication
0.002 - 4
N-(4-methoxyphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0203
N-(4-methylphenyl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.1
N-(4-phenyl-1,3-thiazol-2-yl)benzamide
Escherichia coli
above, pH 7.0, 37°C, recombinant His-tagged enzyme
0.0481
N-(4-[[4-(acetylamino)phenyl]sulfonyl]phenyl)-2-hydroxybenzamide
Plasmodium falciparum
-
-
0.0129
N-(5-chloropyridin-2-yl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0166
N-(7-methyl-1H-indazol-3-yl)-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0094
N-hexadecyl-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0072
N-[(4-methoxyphenyl)methyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0052
N-[3,5-bis(trifluoromethyl)phenyl]-4-[[3,5-bis(trifluoromethyl)phenyl]amino]-3-nitrocyclopenta-1,3-diene-1-sulfonamide
Plasmodium falciparum
-
-
0.0656
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-2-(3-methoxyphenyl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0347
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-2-(4-chlorophenyl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0293
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-2-(4-fluorophenyl)acetamide
Escherichia coli
pH and temperature not specified in the publication
0.0093
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-3-chlorobenzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0066
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-3-methoxybenzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0347
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-4-chlorobenzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.0293
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]-4-fluorobenzamide
Escherichia coli
pH 7.0, 37°C, recombinant His-tagged enzyme
0.1
N-[4-(4-bromophenyl)-1,3-thiazol-2-yl]benzamide
Escherichia coli
above, pH 7.0, 37°C, recombinant His-tagged enzyme
0.0068
N-[4-(trifluoromethyl)phenyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0109
N-[[4-(trifluoromethyl)phenyl]methyl]-3,4-dihydro-2H-1,5-benzodioxepine-7-carboxamide
Escherichia coli
pH and temperature not specified in the publication
0.0394
tert-butyl [4-[(3,4-dihydro-2H-1,5-benzodioxepine-7-carbonyl)amino]phenyl]carbamate
Escherichia coli
pH and temperature not specified in the publication
0.00245
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](2-nitrophenyl)methanone
Escherichia coli
pH and temperature not specified in the publication
0.01668
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](3-methoxyphenyl)methanone
Escherichia coli
pH and temperature not specified in the publication
0.00581
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](3-nitrophenyl)methanone
Escherichia coli
pH and temperature not specified in the publication
0.00668
[5-(2,3-dihydro-1,4-benzodioxin-6-yl)-2-sulfanylidene-1,3,4-oxadiazol-3(2H)-yl](4-nitrophenyl)methanone
Escherichia coli
pH and temperature not specified in the publication
additional information
additional information
Staphylococcus aureus
-
IC50 for platencin is 0.00391 ng/ml
-
0.017
(5R)-4-hydroxy-5-[[4'-(hydroxymethyl)biphenyl-4-yl]methyl]-3,5-dimethylthiophen-2(5H)-one
Mycobacterium tuberculosis
-
-
0.019
(5R)-4-hydroxy-5-[[4'-(hydroxymethyl)biphenyl-4-yl]methyl]-3,5-dimethylthiophen-2(5H)-one
Mycobacterium tuberculosis
-
-
0.006
1-(2,6-dichlorobenzyl)-5-[(3-methoxybenzyl)oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.026
1-(2,6-dichlorobenzyl)-5-[(3-methoxybenzyl)oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.00014
1-(4-carboxybutyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
Escherichia coli
-
-
0.007
1-(4-carboxybutyl)-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
Haemophilus influenzae
-
-
0.0047
1-(5-bromo-2-hydroxybenzyl)-1-(4-chlorophenyl)-3-phenylurea
Escherichia coli
-
pH 7.0, temperature not specified in the publication
0.0047
1-(5-bromo-2-hydroxybenzyl)-1-(4-chlorophenyl)-3-phenylurea
Escherichia coli
pH and temperature not specified in the publication
0.00004
1-[(6-chloro-1,3-benzodioxol-5-yl)methyl]-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
Haemophilus influenzae
-
-
0.00088
1-[(6-chloro-1,3-benzodioxol-5-yl)methyl]-5-[(2,6-dichlorobenzyl)oxy]-1H-indole-2-carboxylic acid
Escherichia coli
-
-
0.007
1-[4-(trifluoromethyl)benzyl]-5-[[4-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.036
1-[4-(trifluoromethyl)benzyl]-5-[[4-(trifluoromethyl)benzyl]oxy]-1H-indole-2-carboxylic acid
Francisella tularensis subsp. holarctica
pH 7.0, 37°C
0.0042
1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0042
1-[5-(4-fluorophenyl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]ethanone
Escherichia coli
pH and temperature not specified in the publication
0.0000088
2-(4-chlorobenzene-1-sulfonyl)naphthalene-1,4-diol
Escherichia coli
pH 7.4, 23°C
0.0001287
2-(4-chlorobenzene-1-sulfonyl)naphthalene-1,4-diol
Plasmodium falciparum
-
pH 7.4, 23°C
0.0001124
2-(4-methylbenzene-1-sulfonyl)anthracene-1,4-diol
Escherichia coli
pH 7.4, 23°C
0.0003411
2-(4-methylbenzene-1-sulfonyl)anthracene-1,4-diol
Plasmodium falciparum
-
pH 7.4, 23°C
0.0000136
2-(4-methylbenzene-1-sulfonyl)naphthalene-1,4-diol
Escherichia coli
pH 7.4, 23°C
0.0000736
2-(4-methylbenzene-1-sulfonyl)naphthalene-1,4-diol
Plasmodium falciparum
-
pH 7.4, 23°C
0.0000097
2-(4-propylbenzene-1-sulfonyl)naphthalene-1,4-diol
Escherichia coli
pH 7.4, 23°C
0.0000726
2-(4-propylbenzene-1-sulfonyl)naphthalene-1,4-diol
Plasmodium falciparum
-
pH 7.4, 23°C
0.0000154
2-(naphthalene-2-sulfonyl)naphthalene-1,4-diol
Escherichia coli
pH 7.4, 23°C
0.000004
2-hydroxy-6-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
Enterococcus faecium
-
-
0.000004
2-hydroxy-6-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
Streptococcus pyogenes
-
-
0.0014
2-hydroxy-6-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
Escherichia coli
-
-
0.0024
2-hydroxy-6-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
Haemophilus influenzae
-
-
0.0038
2-hydroxy-6-[[(2-phenoxybiphenyl-4-yl)carbonyl]amino]benzoic acid
Staphylococcus aureus
-
-
0.0000465
3-(1,4-dihydroxynaphthalene-2-sulfonyl)propanoic acid
Plasmodium falciparum
-
pH 7.4, 23°C
0.0000965
3-(1,4-dihydroxynaphthalene-2-sulfonyl)propanoic acid
Escherichia coli
pH 7.4, 23°C
0.0019
3-(2-phenylethyl)-1,3-thiazolidin-2-one 1,1-dioxide
Escherichia coli
IC50: 0.0019 mM
0.0216
3-(2-phenylethyl)-1,3-thiazolidin-2-one 1,1-dioxide
Plasmodium falciparum
-
IC50: 0.0216 mM
0.0009
3-(biphenyl-4-ylmethyl)-1,3-thiazolidin-2-one 1,1-dioxide
Escherichia coli
IC50: 0.0009 mM
0.0494
3-(biphenyl-4-ylmethyl)-1,3-thiazolidin-2-one 1,1-dioxide
Plasmodium falciparum
-
IC50: 0.0494 mM
0.0053
3-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2-thione
Plasmodium falciparum
-
IC50: 0.0053 mM
0.0177
3-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2-thione
Escherichia coli
IC50: 0.0177 mM
0.0556
3-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2-thione
Plasmodium falciparum
-
IC50: 0.0556 mM
0.1
3-(biphenyl-4-ylmethyl)-1,3-thiazolidine-2-thione
Escherichia coli
IC50: 0.1 mM, above
0.0734
3-(pyridin-3-ylmethyl)-1,3-thiazolidine-2-thione
Plasmodium falciparum
-
IC50: 0.0734 mM
0.1
3-(pyridin-3-ylmethyl)-1,3-thiazolidine-2-thione
Escherichia coli
IC50: 0.1 mM, above
0.0024
3-[(4'-cyclopentylbiphenyl-4-yl)methyl]-1,3-thiazolidin-2-one 1,1-dioxide
Escherichia coli
IC50: 0.0024 mM
0.0108
3-[(4'-cyclopentylbiphenyl-4-yl)methyl]-1,3-thiazolidin-2-one 1,1-dioxide
Plasmodium falciparum
-
IC50: 0.0108 mM
0.0024
3-[4-(4-cyclopentylphenoxy)benzyl]-1,3-thiazolidin-2-one 1,1-dioxide
Escherichia coli
-
0.0108
3-[4-(4-cyclopentylphenoxy)benzyl]-1,3-thiazolidin-2-one 1,1-dioxide
Plasmodium falciparum
-
-
0.0053
3-[4-(4-cyclopentylphenoxy)benzyl]-1,3-thiazolidine-2-thione
Plasmodium falciparum
-
-
0.0177
3-[4-(4-cyclopentylphenoxy)benzyl]-1,3-thiazolidine-2-thione
Escherichia coli
-
0.0111
4-(4-biphenyl-4-ylcyclohexyl)-1,3-thiazolidin-2-one
Plasmodium falciparum
-
IC50: 0.0111 mM
0.0144
4-(4-biphenyl-4-ylcyclohexyl)-1,3-thiazolidin-2-one
Escherichia coli
IC50: 0.0144 mM
0.0053
4-(4-biphenyl-4-ylcyclohexyl)-1,3-thiazolidine-2-thione
Plasmodium falciparum
-
IC50: 0.0053 mM
0.0177
4-(4-biphenyl-4-ylcyclohexyl)-1,3-thiazolidine-2-thione
Escherichia coli
IC50: 0.0177 mM
0.0000118
[4-(1,4-dihydroxynaphthalene-2-sulfonyl)phenyl]carbamic acid
Escherichia coli
pH 7.4, 23°C
0.0000296
[4-(1,4-dihydroxynaphthalene-2-sulfonyl)phenyl]carbamic acid
Plasmodium falciparum
-
pH 7.4, 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000006
-
purified recombinant enzyme, primer substrate 2-methylcrotonyl-CoA
0.000015
-
purified recombinant enzyme, primer substrate isovaleryl-CoA
0.000031
-
purified recombinant enzyme, primer substrate isobutyryl-CoA
0.00013
0.005
purified recombinant enzyme, substrates acetyl-CoA and malonyl-[acyl-carrier-protein]
0.0062
-
transgenic leaves transformed with the Cuphea glaucescens enzyme, average value
0.024
acetoacetyl-ACP synthase activity, recombinant strain JT2038
additional information
0.00013
acetyl transacetylase activity, recombinant strain JT2038
additional information
-
activity of wild-type embryo and those from transgenic plants
additional information
activity of the recombinant wild-type or N291D mutant enzymes in seed extracts of Brassica napus and of Cuphea lanceolata
additional information
activity of the recombinant wild-type or N291D mutant enzymes in seed extracts of Brassica napus and of Cuphea lanceolata
additional information
-
activity of the recombinant wild-type or N291D mutant enzymes in seed extracts of Brassica napus and of Cuphea lanceolata
additional information
activity of the recombinant wild-type or mutant N291D enzymes in seed extracts of Brassica napus and of Cuphea lanceolata
additional information
activity of the recombinant wild-type or mutant N291D enzymes in seed extracts of Brassica napus and of Cuphea lanceolata
additional information
-
activity of the recombinant wild-type or mutant N291D enzymes in seed extracts of Brassica napus and of Cuphea lanceolata
additional information
-
analysis of fatty acid content of the wild-type strain
additional information
-
substrate specificity of the purified His-tagged enzyme
additional information
-
assay for the Mycobacterium tuberculosis FabH (mtFabH) enzyme involved in a key initiation step in the synthesis of mycolic acids, which are an integral component of the cell wall. The assay eliminates the need for the cumbersome washing steps or specialty scintillation proximity assay beads and the preparation of acyl-carrier proteins required in other assay formats. This discontinuous assay involves the reduction of radiolabled long-chain beta-ketoacyl CoA product to its dihydroxy derivative, which partitions into a nonpolar phase for quantitation, while the reduced radiolabeled substrate derivative remains in the aqueous phase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
7.6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme KASIIIA, chloroplast precursor; isozyme KASIIIa
SwissProt
brenda
-
-
-
brenda
wild type and C122A mtFabH proteins are overexpressed in Escherichia coli with N-terminal polyhistidine tag
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
constitutive expression of isozymes KAS III-1 and KAS III-2
brenda
additional information
-
JcKAS III is expressed in all tissues examined with highest expression in roots
brenda
-
developing, constitutive expression of isozymes KAS III-1 and KAS III-2
brenda
equal expression of the isozyme in early stages of development and during maturation
brenda
equal expression of isozyme KAS3a in early stages of development and during maturation
brenda
additional information
-
quantitatiev RT-PCR expression analysis of isozymes KAS III-1 and KAS III-2
brenda
additional information
development-specific expression of isozymes
brenda
additional information
development-specific expression of isozymes
brenda
additional information
-
development-specific expression of isozymes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids
evolution
enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids
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
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
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
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
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
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
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
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
-
evolution
-
enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids
-
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
-
malfunction
-
enzyme loss reduces the production of an acyl homoserine lactone quorum-sensing signal. Deletion of the enzyme supports the redirection of acyl-acyl-carrier protein toward biosurfactant synthesis, which in turn enhances swarming motility
malfunction
-
isoform fabH2 gene deletion does not cause significant changes in the growth or fatty acid composition of Streptomyces coelicolor
malfunction
-
isoform fabH2 gene deletion does not cause significant changes in the growth or fatty acid composition of Streptomyces coelicolor
-
malfunction
-
enzyme loss reduces the production of an acyl homoserine lactone quorum-sensing signal. Deletion of the enzyme supports the redirection of acyl-acyl-carrier protein toward biosurfactant synthesis, which in turn enhances swarming motility
-
metabolism
beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
metabolism
-
KASIII is involved in the biosynthesis of short-chain-length/medium-chain-length polyhydroxyalkanoate, pathway overview
metabolism
B1XPH5
the initiation ketosynthase FabH is the sole rate-limiting enzyme of the fatty acid synthesis of Synechococcus sp. PCC 700. Reconstitution of the fatty acid synthase system, FAS. FabH ketosynthase initiates product synthesis by condensing malonyl-ACP with acetyl-CoA to form acetoacetyl-ACP
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
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
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
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
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
metabolism
the beta-ketoacyl-acyl carrier protein (ACP) synthases, FabB, FabF, and FabH, catalyse the Claisen condensation of fatty acyl-thioesters and malonyl-ACP to form a 3-oxoacyl-ACP intermediate elongated by two carbon atoms. The initial cycle of elongation is catalysed by FabH, involving condensation of malonyl-ACP and acetyl-CoA, while subsequent cycles of elongation are performed by FabB or FabF
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
metabolism
enzyme FabH catalyzes the initiation reaction of fatty acid biosynthesis
metabolism
FabB, FabF, and FabH are the condensing enzymes in te fatty acid synthesis system FAS II that play an important role in the initiation and elongation of fatty acid chains. FabB and FabF use acyl-ACPs as primers, while FabH uses acetyl-CoA as an acyl donor, which makes it unique among the FAS II condensing enymes
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
metabolism
-
the enzyme is involved in the biosynthesis of asukamycin
metabolism
-
the enzyme is involved in the biosynthesis of FK506
metabolism
-
the enzyme is involved in the biosynthesis of reveromycin
metabolism
the enzyme is involved in the biosynthesis of alkylquinolone
metabolism
-
the enzyme is involved in the biosynthesis of corallopyronin
metabolism
-
the enzyme is involved in the biosynthesis of 2,5-dialkylresorcinol
metabolism
-
the enzyme is involved in the biosynthesis of lipstatin
metabolism
-
the enzyme is involved in the biosynthesis of tetronomycin
metabolism
-
the enzyme is involved in the biosynthesis of kijanimicin
metabolism
-
the enzyme is involved in the biosynthesis of mevalonate/terpenoid
metabolism
-
the enzyme is involved in the biosynthesis of tetracycline SF2575n
metabolism
-
the enzyme is involved in the biosynthesis of chlorothricin
metabolism
-
the enzyme is involved in the biosynthesis of daunorubicin
metabolism
-
the enzyme is involved in the biosynthesis of avilamycin
metabolism
-
the enzyme is involved in the biosynthesis of evernimicin
metabolism
-
the enzyme is involved in the biosynthesis of calicheamicin
metabolism
-
the enzyme is involved in the biosynthesis of tiacumicin
metabolism
-
the enzyme is involved in the biosynthesis of tiacumicin
metabolism
-
the enzyme is involved in the biosynthesis of esmeraldin
metabolism
-
the enzyme is involved in the biosynthesis of A33853
metabolism
enzyme overexpression increases pinocembrin production in recombinant Escherichia coli
metabolism
-
the enzyme is involved in the biosynthesis of aclacinomycin
metabolism
-
isoforms FabH1 and FabH2 have major roles in straight-chain fatty acid and branched-chain fatty acid biosynthesis, respectively
metabolism
-
the LstAB protein plays a role in the biosynthesis of lipstatin
metabolism
-
the enzyme is involved in the biosynthesis of benastatin
metabolism
-
the enzyme is involved in the biosynthesis of frenolicin
metabolism
-
the enzyme is involved in the biosynthesis of fredericamycin
metabolism
-
the enzyme is involved in the biosynthesis of hedamycin
metabolism
-
the enzyme is involved in the biosynthesis of undecylprodiginine
metabolism
-
isoforms AsuC3 and AsuC4 are involved in the biosynthesis of the upper triene chain of asukamycin and capable of both catalyzing the condensation between free acyl-CoA/malonyl-acyl-carrier protein (ACP) (initiation) and acyl-ACP/malonyl-ACP (elongation)
metabolism
-
isoform FabH2 plays a minor role in fatty acid synthesis and is not critical for actinorhodin and undecylprodigiosin production
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
-
metabolism
-
beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
-
metabolism
-
isoform FabH2 plays a minor role in fatty acid synthesis and is not critical for actinorhodin and undecylprodigiosin production
-
metabolism
-
the initiation ketosynthase FabH is the sole rate-limiting enzyme of the fatty acid synthesis of Synechococcus sp. PCC 700. Reconstitution of the fatty acid synthase system, FAS. FabH ketosynthase initiates product synthesis by condensing malonyl-ACP with acetyl-CoA to form acetoacetyl-ACP
-
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
-
metabolism
-
isoforms FabH1 and FabH2 have major roles in straight-chain fatty acid and branched-chain fatty acid biosynthesis, respectively
-
metabolism
-
the enzyme is involved in the biosynthesis of abyssomicin
-
metabolism
-
the enzyme is involved in the biosynthesis of corallopyronin
-
metabolism
-
the enzyme is involved in the biosynthesis of 2,5-dialkylresorcinol
-
metabolism
-
the enzyme is involved in the biosynthesis of kijanimicin
-
metabolism
Polymorphospora rubra K07-0510
-
the enzyme is involved in the biosynthesis of trehangelin
-
metabolism
Streptomyces antibioticus DSM 4072
-
the enzyme is involved in the biosynthesis of chlorothricin
-
metabolism
Streptomyces antibioticus DSM 4072
-
the enzyme is involved in the biosynthesis of esmeraldin
-
metabolism
-
the enzyme is involved in the biosynthesis of pactamycin
-
metabolism
-
the enzyme is involved in the biosynthesis of avilamycin
-
metabolism
-
the enzyme is involved in the biosynthesis of calicheamicin
-
metabolism
-
the enzyme is involved in the biosynthesis of tiacumicin
-
metabolism
Streptomyces antibioticus Tue2706
-
the enzyme is involved in the biosynthesis of chlorothricin
-
metabolism
Streptomyces antibioticus Tue2706
-
the enzyme is involved in the biosynthesis of esmeraldin
-
metabolism
Streptomyces galilaeus 3AR-33
-
the enzyme is involved in the biosynthesis of aclacinomycin
-
metabolism
Streptomyces roseofulvus AM-3867
-
the enzyme is involved in the biosynthesis of frenolicin
-
metabolism
Streptomyces griseus ATCC 49344
-
the enzyme is involved in the biosynthesis of fredericamycin
-
metabolism
-
the enzyme is involved in the biosynthesis of undecylprodiginine
-
physiological function
FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP. FabH represents a potential regulatory key point of the mycolic acid pathway
physiological function
-
the enzyme plays an important role in fatty acid synthesis initiation in Plasmodium falciparum, overview
physiological function
FabH initiates elongation in fatty acid synthesis FAS-II, type II fatty acid biosynthesis pathway overview
physiological function
-
FabH is an important enzyme in the elongation steps of fatty-acid biosynthesis
physiological function
-
KAS III is a condensing enzyme that initiates fatty acid biosynthesis
physiological function
-
FabH is central to the initiation of fatty acid biosynthesis
physiological function
-
beta-ketoacyl-acyl carrier protein synthase is a condensing enzyme catalyzing the initial elongation step of type II fatty acid biosynthetic process and acyl carrier protein (ACP) facilitates the shuttling of the fatty acyl intermediates to the active site of the respective enzymes in the pathway
physiological function
beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP
physiological function
beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP
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
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
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
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
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
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
physiological function
beta-ketoacyl-ACP-synthase III is a key condensing enzyme in the type II fatty acid synthesis system. The pathway in bacteria is essential for growth and survival
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
physiological function
-
Pseudomonas syringae strain B728a uses the enzyme isoform FabH1 to provide the critical fatty acid precursor butyryl-[acyl-carrier protein] for acyl homoserine lactone synthesis. Isoform FabH2 is able to function in redirecting intermediates from beta-oxidation to fatty acid synthesis. Both isoforms FabH1 and FabH2 are not essential for de novo fatty acid synthesis. Isoform FabH1 is not essential for cell membrane stability in Pseudomonas syringae. Isoform FabH1 affects swarming motility and biosurfactant production in Pseudomonas syringae
physiological function
-
the enzyme isoform FabH2 is nonessential for growth and fatty acid biosynthesis. Isoform fabH2 overexpression reduces the blue-pigmented actinorhodin production
physiological function
-
FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP. FabH represents a potential regulatory key point of the mycolic acid pathway
-
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
-
physiological function
-
beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP
-
physiological function
-
the enzyme isoform FabH2 is nonessential for growth and fatty acid biosynthesis. Isoform fabH2 overexpression reduces the blue-pigmented actinorhodin production
-
physiological function
-
FabH is an important enzyme in the elongation steps of fatty-acid biosynthesis
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physiological function
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Pseudomonas syringae strain B728a uses the enzyme isoform FabH1 to provide the critical fatty acid precursor butyryl-[acyl-carrier protein] for acyl homoserine lactone synthesis. Isoform FabH2 is able to function in redirecting intermediates from beta-oxidation to fatty acid synthesis. Both isoforms FabH1 and FabH2 are not essential for de novo fatty acid synthesis. Isoform FabH1 is not essential for cell membrane stability in Pseudomonas syringae. Isoform FabH1 affects swarming motility and biosurfactant production in Pseudomonas syringae
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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
-
additional information
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three-dimensional structure analysis, homology modeling and docking studies of beta-ketoacyl-ACP synthase III, FabH, enzyme involved in type II fatty acid biosynthesis of Chlorella variabilis, protein-protein docking and molecular dynamics simulation protocols. The FabH-ACP complex has the lowest docking energy score and shows the binding of ACP to the electropositive FabH surface with strong hydrogen bond interactions. The substrate-complexed FabH adopts a more stable conformation than the free enzyme. The FabH structure retains its stability throughout the simulation although noticeable displacements are observed in the loop regions. Molecular simulation studies suggest the importance of crucial hydrogen bonding of the conserved Arg91 of FabH with Glu53 and Asp56 of ACP for exhibiting high affinity between the enzyme and substrate
additional information
molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 1MZS, with a bound indole analogue inhibitor, to start. Analysis of protein-ligand interactions in the ecFabH co-crystal structure
additional information
molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 3IL5 to start. Analysis of protein-ligand interactions in the efFabH co-crystal structure
additional information
active site and substrate binding, ligand binding, molecular dynamics simulations and binding site mapping, detailed overview
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
enzyme structure and active site architecture, comparison with FabF, EC 2.3.1.179. Possible substrate and inhibitor interactions of Yersinia pestis FabH, Arg151 of YpFabH clashes with the adenine ring of CoA
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
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FabH has a catalytic triad of Cys112/His244/Asn274
-
additional information
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molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 3IL5 to start. Analysis of protein-ligand interactions in the efFabH co-crystal structure
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additional information
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FabH has a catalytic triad of Cys112/His244/Asn274
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additional information
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active site and substrate binding, ligand binding, molecular dynamics simulations and binding site mapping, detailed overview
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Show AA Sequence and Transmembrane Helices (19923 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33516
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2 * 33516, amino acid sequence calculation, 2 * 33889, selenomethionine-labeled recombinant enzyme, mass spectrometry
33517
x * 33517, DNA sequence calculation, x * 34800, recombinant enzyme, SDS-PAGE
33889
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2 * 33516, amino acid sequence calculation, 2 * 33889, selenomethionine-labeled recombinant enzyme, mass spectrometry
34800
x * 33517, DNA sequence calculation, x * 34800, recombinant enzyme, SDS-PAGE
35000
37000
42000
43000
35000
2 * 35000, structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, overview
42000
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x * 42000, about, amino acid sequence calculation, isozyme KAS III-1, x * 43000, about, amino acid sequence calculation, isozyme KAS III-2
43000
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x * 42000, about, amino acid sequence calculation, isozyme KAS III-1, x * 43000, about, amino acid sequence calculation, isozyme KAS III-2
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
?
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x * 42000, about, amino acid sequence calculation, isozyme KAS III-1, x * 43000, about, amino acid sequence calculation, isozyme KAS III-2
?
x * 33517, DNA sequence calculation, x * 34800, recombinant enzyme, SDS-PAGE
?
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x * 35000, recombinant His-tagged enzyme, SDS-PAGE
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dimer
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2 * 33516, amino acid sequence calculation, 2 * 33889, selenomethionine-labeled recombinant enzyme, mass spectrometry
dimer
the YpFabH monomer contains 10 alpha-helices and 14 beta-strands, the core motif of YpFabH contains a characteristic thiolase fold, monomer interaction analysis, dimer interface structure, and structure comparison with FabF, EC 2.3.1.179
homodimer
2 * 35000, structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, overview
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
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two thirds of the monomer are a highly structured alpha/beta motif, secondary structure, overview
additional information
three-dimensional structure analysis, the enzyme contains a large solvent-accessible channel in the dimer interface as well as two cis-peptides, cis-Pro88 and cis-Phe308, in two of the disordered loops, structural instability
additional information
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three-dimensional structure analysis, the enzyme contains a large solvent-accessible channel in the dimer interface as well as two cis-peptides, cis-Pro88 and cis-Phe308, in two of the disordered loops, structural instability
additional information
structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, detailed overview. Residues required for intersubunit stability are Phe87 and its complementary residues from the adjacent monomer, Thr190, Leu191, Pro192, Asn193. The active site is composed of a catalytic triad formed by residues, Cys112, His244, and Asn274. Residue Cys112 is involved in acetyl transfer, while His244 and Asn274 play an active role in decarboxylation. Residues His244 and Asn274 are present close to Cys112 in the long active site tunnel. Cysteine 112 lies on the bottom of the active-site tunnel, the entrance of which is flanked by residues Trp32 and Arg151
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
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FabH has a catalytic triad of Cys112/His244/Asn274
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additional information
secondary structure elements of the FabH protein, comparison with the enzyme from Enterococcus faecalis, overview
additional information
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secondary structure elements of the FabH protein, comparison with the enzyme from Enterococcus faecalis, overview
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additional information
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structure-function relationship, overview
additional information
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structure-function relationship, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
FabH is efficiently phosphorylated in vitro exclusively on Thr45 by several mycobacterial Ser/Thr protein kinases, particularly by PknF and PknA, as well as in vivo in mycobacteria, mass spectrometric analysis, overview. Mapping of the Thr45 phosphorylation site on the FabH crystal structure
phosphoprotein
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FabH is efficiently phosphorylated in vitro exclusively on Thr45 by several mycobacterial Ser/Thr protein kinases, particularly by PknF and PknA, as well as in vivo in mycobacteria, mass spectrometric analysis, overview. Mapping of the Thr45 phosphorylation site on the FabH crystal structure
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme or mutant enzymes C155A, C264A and C155A/C264A in complex with octanoyl-CoA, using PEG3350 as a precipitant and Tris HCl buffer (pH 7.0-8.0) and 0.1 M calcium acetate
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purified recombinant free enzyme, hanging drop vapour diffusion method, 20 mg/ml protein at 15°C with 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 6.5, 25% PEG 3350, enzyme mutant D36A/E37A with 2-[4-(3,5-dimethylpiperidin-1-yl)-3-phenoxybenzoylamino]benzoic acid, in 25% PEG 3350, 0.2 M ammonium sulfate, and 0.1 M Bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 1.8 A resolution
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cyrstals of ecFabH and the ecFabH/methyl-CoA disulfide complex are obtained by the hanging drop method
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purified FabH as apoenzyme or ligand-bound complex, X-ray diffraction structure determination and analysis at 1.46 A resolution
purified FabH as apoenzyme or with bound acetyl-CoA, structure and reaction mechanism modeling
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purified recombinant His-tagged, selenomethionine-labeled wild-type enzyme, hanging drop vapour diffusion method, 15 mg/ml protein in 20 mM Tris, pH 7.4, 1 mM EDTA, and 1 mM DTT, crystallization solution contains 1.8-2.0 M ammonium acetate, 2% PEG 400, 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8-2.5 A resolution, modeling
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purified recombinant selenomethionine-labeled enzyme, 0.002 ml of 13 mg/ml protein in 20 mM Tris, pH 7.5, 50 mM NaCl, 10 mM DTT, and 4 mM acetyl-CoA, versus 0.002 ml reservoir solution containing 12-14% PEG 4000, 40 mM Bis-Tris propane, pH 7.0, and 80 mM magnesium acetate, overnight, X-ray diffraction structure determination and analysis at 1.9 A resolution
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sitting-drop vapor-diffusion method, pH 9.0, 10% PEG 200, 18% PEG 8000
crystallization of the mtFabH/decyl-CoA disulfide is achieved using the hanging-drop vapour-diffusion technique. The active site cysteine in both subunits of the wild type mtFabH dimer is able to react with either a dodecanoyl-CoA substrate or a decyl-CoA disulfide inhibitor
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hanging-drop vapor diffusion method, crystal structures of mtFabH and C112A mtFabH with 1
mapping of the Thr45 phosphorylation site on the mtFabH crystal structure, overview
purified FabH, X-ray diffraction structure determination and analysis at 2.1 A resolution
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purified recombinant enzyme in complex with lauroyl-CoA, X-ray diffraction structure determination and analysis at 1.85-2.3 A resolution, modeling
purified recombinant mutant enzymes R46A/R161A and W42A/R163A, 0.003 ml R46A/R161A solution containing 20 mg/ml protein, 20 mM Tris-HCl, pH 7.5, 0.5 M NaCl, 2 mM 2-mercaptoethanol, 10% glycerol, mixed with 0.001 ml of crystallization solution containing 0.1 M HEPES, pH 7.5, 10% v/v isopropyl alcohol, 20% w/v PEG 4000, for the W42A/R163A solution 0.002 ml of protein solution is mixed with 0.001 ml of crystallization solution containing 0.2 M ammonium sulfate, and 30% w/v PEG 8000, X-ray diffraction structure determination and analysis at 2.0-2.65 A resolution
15 mg/ml purified enzyme in 20 mM Tris, pH 8.0, 3 mM DTT, 100 mM NaCl, 10% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution
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sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.0, and 1.4 M sodium acetate-trihydrate
purified recombinant His-tagged KASIII, by sitting-drop vapour-diffusion method, 4 mg/ml proteinin 25 mM Tris-HCl, pH 7.5, 20% glycerol, 3 mM 2-mercaptoethanol, 1 M NaCl is mixed with precipitatnt solution containing 0.1 M HEPES, pH 7.2, 30% PEG 6000, 5% 2-methyl-2,4-pentanediol and 3% D-galactose, X-ray diffraction structure determination and analysis at 2.05 A resolution
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purified recombinant enzyme in apoform or as acetylated enzyme, hanging drop vapour diffusion technique, mixing of 0.0015 ml of 20 mg/ml protein solution with an equal amount of reservoir solution, containing 10% propan-2-ol, 0.1 M HEPES, pH 7.5, 15% glycerol, 24% PEG 4000, and equilibration against 0.3 ml of reservoir solution, 13°C, acetylated-YpFabH by co-crystallisation with acetyl-CoA at a molar ratio of 5:5:1 of acetyl-CoA-malonyl-CoA-YpFabH at 10 mg/ml protein, X-ray diffraction structure determination and analysis at 18-2.2 A resolution, molecular replacement using the enzyme structure of Escherichia coli, PDB ID 1HN9, as search model
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F260Q
the mutant shows reduced binding ability to inhibitors YKab-4 and YKab-6 as compared to the wild type enzyme
F56W
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the mutation does not show a drastic change in reactivity towards octanoyl-CoA even though the band of the variant is reduced approximately by 40% compared to the wild type
I198Q
the mutant shows reduced binding ability to inhibitors YKab-4 and YKab-6 as compared to the wild type enzyme
A294S
site-directed mutagenesis, the mutant enzyme shows reduced activity and reduced sensitivity to decanoyl-ACP inhibition compared to the wild-type
A295P
site-directed mutagenesis, the mutant enzyme shows reduced activity and reduced sensitivity to decanoyl-ACP inhibition compared to the wild-type
C111A
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site-directed mutagenesis, the mutant enzyme loses all condensing activity
C111S
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site-directed mutagenesis, the mutant enzyme loses all condensing activity, but is still able to bind acetyl-CoA and malonyl-ACP and to decarboxylate the latter to acetyl-ACP
C111S/H261A
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site-directed mutagenesis, the mutant enzyme loses all condensing activity
C111S/H261R
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site-directed mutagenesis, the mutant enzyme loses all condensing activity, but is still able to bind acetyl-CoA and malonyl-ACP and to decarboxylate the latter to acetyl-ACP
H261A
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site-directed mutagenesis, the mutant enzyme loses all condensing activity
H261R
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site-directed mutagenesis, the mutant enzyme shows reduced condensing activity compared to the wild-type enzyme
N291D
site-directed mutagenesis, the mutant enzyme shows reduced activity and reduced sensitivity to decanoyl-ACP inhibition compared to the wild-type
R150A
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site-directed mutagenesis, the mutant enzyme shows reduced condensing activity compared to the wild-type enzyme
R266A
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site-directed mutagenesis, the mutant enzyme shows reduced condensing activity compared to the wild-type enzyme
R306A
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site-directed mutagenesis, the mutant enzyme shows highly reduced condensing activity compared to the wild-type enzyme
C112S
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site-directed mutagenesis, the mutant enzyme shows abolished condensation and transacylation activities, but 4fold increased decarboxylation activity compared to the wild-type enzyme
F87A
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87C
F87C/H244A
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H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87D
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87E
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87G
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87H
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87I
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87I/H244A
-
H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87K
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87L
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87M
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87N
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87P
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87Q
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87R
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain does not confer the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87S
F87S/N274A
-
N274 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87T
F87T/H244A
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H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
F87V
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site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli does not confer the ability to synthesize polyhydroxyalkanoates, overview
F87W
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87Y
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
H244A
H244A/N274A
-
N274 and H244 play key roles in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
N274A
C122A
site-directed mutagenesis, the mutant shows 0.25% of wild-type enzyme condensation activity, and 2.4% of wild-type malonyl-ACP decarboxylation activity
H258A
site-directed mutagenesis, the mutant shows 0.46% of wild-type enzyme condensation activity, and 0.68% of wild-type malonyl-ACP decarboxylation activity
N289A
site-directed mutagenesis, the mutant shows 0.51% of wild-type enzyme condensation activity, and 2.24% of wild-type malonyl-ACP decarboxylation activity
R161A
site-directed mutagenesis, the mutant shows 69.7% of wild-type enzyme condensation activity, and 8.7% of wild-type malonyl-ACP decarboxylation activity
R46A
site-directed mutagenesis, the mutant shows 7.3% of wild-type enzyme condensation activity, and 0.79% of wild-type malonyl-ACP decarboxylation activity
R46A/R161A
site-directed mutagenesis, the mutant shows 0.31% of wild-type enzyme condensation activity, and 5.1% of wild-type malonyl-ACP decarboxylation activity
T45A
the mutant exhibits slightly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
T45D
the mutant exhibits markedly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
T97F
site-directed mutagenesis, the mutant shows 0.47% of wild-type enzyme condensation activity, and 0.84% of wild-type malonyl-ACP decarboxylation activity
W42A
site-directed mutagenesis, the mutant shows 21.6% of wild-type enzyme condensation activity, and 30.1% of wild-type malonyl-ACP decarboxylation activity
W42A/R161A
site-directed mutagenesis, the mutant shows 0.24% of wild-type enzyme condensation activity, and 9.7% of wild-type malonyl-ACP decarboxylation activity
C122A
-
site-directed mutagenesis, the mutant shows 0.25% of wild-type enzyme condensation activity, and 2.4% of wild-type malonyl-ACP decarboxylation activity
-
R161A
-
site-directed mutagenesis, the mutant shows 69.7% of wild-type enzyme condensation activity, and 8.7% of wild-type malonyl-ACP decarboxylation activity
-
R46A
-
site-directed mutagenesis, the mutant shows 7.3% of wild-type enzyme condensation activity, and 0.79% of wild-type malonyl-ACP decarboxylation activity
-
T45A
-
the mutant exhibits slightly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
-
T45D
-
the mutant exhibits markedly decreased transacylation, malonyl-AcpM decarboxylation, and condensing activities compared to the wild-type protein
-
T97F
-
site-directed mutagenesis, the mutant shows 0.47% of wild-type enzyme condensation activity, and 0.84% of wild-type malonyl-ACP decarboxylation activity
-
W42A
-
site-directed mutagenesis, the mutant shows 21.6% of wild-type enzyme condensation activity, and 30.1% of wild-type malonyl-ACP decarboxylation activity
-
C122A
-
site-directed mutagenesis, the mutant enzyme expressed in Streptomyces glaucescens generates 75% more straight-chain fatty acids than the wild-type enzyme, plasmid-based expression does not affect Escherichia coli strain TG-2, the mutation causes uncoupling of condensation and decarboxylation reactions
C122Q
-
site-directed mutagenesis, the mutant enzyme expressed in Streptomyces glaucescens generates 500% more straight-chain fatty acids than the wild-type enzyme, plasmid-based expression does not affect Escherichia coli strain TG-2, the mutation causes uncoupling of condensation and decarboxylation reactions
C122S
-
site-directed mutagenesis, the mutant enzyme expressed in Streptomyces glaucescens generates 100% more straight-chain fatty acids than the wild-type enzyme, plasmid-based expression does not affect Escherichia coli strain TG-2, the mutation causes uncoupling of condensation and decarboxylation reactions
additional information
F87C
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87S
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87T
-
site-directed mutagenesis, coexpression of the mutant enzyme with the phaC gene from Aeromonas caviae in a recombinant strain confers the ability to synthesize polyhydroxyalkanoates, coexpression of the mutant with gene phaC1 from Pseudomonas sp. strain 61-3 in Escherichia coli confers the ability to synthesize polyhydroxyalkanoates, overview
F87T
-
coexpression of the enzyme in Arabidopsis thaliana plastids with Ser325Thr/Gln481Lys mutated polyhydroxyalkanoate synthase from Pseudomonas sp. 61-3, along with the beta-ketothiolase PhaA and acetoacetyl-CoA reductase PhaB from Ralstonia eutropha for successful production of short-chain-length/medium-chain-length polyhydroxyalkanoates in the transgenic plant plastids, expression of the engineered fabH gene in the plastid leads to an increase in the amount of the SCL monomer, 3-hydroxybutyrate, incorporated into polyhydroxyalkanoates, and contributes to supply of medium-chain-length monomers for polyhydroxyalkanoate production, overview
H244A
-
site-directed mutagenesis, the mutant enzyme shows strongly reduced condensation and decarboxylation activities, but 6fold increased transacylation activity compared to the wild-type enzyme
H244A
-
H244 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding, in the mutant stabilization is reduced inhibiting the condensation reaction, leading to an increase in transacylase activity, allowing larger substrates to be subjected to acyl-ACP to acyl-CoA transacylation
N274A
-
site-directed mutagenesis, the mutant enzyme shows strongly reduced condensation and decarboxylation activities, but about 20% increased transacylation activity compared to the wild-type enzyme
N274A
-
N274 plays a key role in stabilizing the oxyanion generated in the condensation reaction through hydrogen bonding
additional information
-
coexpression of the KASIII mutant F87T enzyme from Escherichia coli in Arabidopsis thaliana plastids together with Ser325Thr/Gln481Lys mutated polyhydroxyalkanoate synthase from Pseudomonas sp. 61-3, along with the beta-ketothiolase PhaA and acetoacetyl-CoA reductase PhaB from Ralstonia eutropha for successful production of short-chain-length/medium-chain-length polyhydroxyalkanoates in the transgenic plant plastids, expression of the engineered Escherichia coli fabH gene in the plastid leads to an increase in the amount of the SCL monomer, 3-hydroxybutyrate, incorporated into polyhydroxyalkanoates, and contributes to supply of medium-chain-length monomers for polyhydroxyalkanoate production, overview
additional information
-
transfection with Cuphea glaucescens isozymes KAS III-1 and KAS III-2 leads to altered fatty acid levels with accumulation of palmitate
additional information
-
analysis of fatty acid composition and acyl-ACP content of transgenic plants expressing the two isozymes of Cuphea glaucescens, the transgenic plants show altered fatty acid levels with accumulation of palmitate
additional information
-
construction of an enzyme-deficient null mutant strain in which the gene encoding the enzyme from Salmonella enterica serovar typhimurium is inserted as a single copy or in two copies, removal of one of the two copies reduces enzyme activity, removal of the single copy of the gene leads to cell death revealing that the enzyme is absolutely essential for viability, overview
additional information
-
construction of transgenic Brassica napus plants overexpressing the Escherichia coli enzyme in seeds, expression analysis during seed adevelopment
additional information
-
construction of an enzyme-deficient null mutant strain CL112 by in-frame deletion of FabH active site region, the mutant strain requires unsaturated, but not saturated, long-chain fatty acids for growth, and retains about 10% of wild-type acetate incorporation and fatty acid synthesis activity leading to synthesis of branched-chain fatty acids, analysis of fatty acid content of the mutant strain, overview
additional information
-
construction of an enzyme-deficient null mutant strain CL112 by in-frame deletion of FabH active site region, the mutant strain requires unsaturated, but not saturated, long-chain fatty acids for growth, and retains about 10% of wild-type acetate incorporation and fatty acid synthesis activity leading to synthesis of branched-chain fatty acids, analysis of fatty acid content of the mutant strain, overview
-
additional information
-
transfections with Cuphea glaucescens isozymes KAS III-1 and KAS III-2 or the spinach enzyme lead to altered fatty acid levels with accumulation of palmitate
additional information
-
mutagenic replacement of the chromosomal endogenous enzyme by a plasmid-encoded Escherichia coli enzyme leads to a highly altered fatty acid profile in Streptomyces coelicolor, while plasmid-encoded expression of the Streptomyces glaucescens enzyme alters the fatty acid profile only slightly, overview
additional information
B1XPH5
the Synechococcus FabH is used for replacement of its counterpart in the reconstituted Escherichia coli fatty acid synthase system, the resulting complex is strongly limited in FabH activity. The introduction of the Escherichia coli FabH enzyme into the Synechococcus fatty acid synthase system virtually eliminates its dependence on the FabH subunit
additional information
-
the Synechococcus FabH is used for replacement of its counterpart in the reconstituted Escherichia coli fatty acid synthase system, the resulting complex is strongly limited in FabH activity. The introduction of the Escherichia coli FabH enzyme into the Synechococcus fatty acid synthase system virtually eliminates its dependence on the FabH subunit
additional information
-
the Synechococcus FabH is used for replacement of its counterpart in the reconstituted Escherichia coli fatty acid synthase system, the resulting complex is strongly limited in FabH activity. The introduction of the Escherichia coli FabH enzyme into the Synechococcus fatty acid synthase system virtually eliminates its dependence on the FabH subunit
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
unfolding of the recombinant selenomethionine-labeld enzyme starts above
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified enzyme, 20 mM Tris buffer, 1 mM DTT, 20% glycerol, 0.01% Triton X-100, several weeks with slight loss of activity
-
4°C, free enzyme in 20 mM Tris (pH 7.6), 10 days, almost complete loss of activity
-
4°C, immobilized enzyme in 20 mM Tris (pH 7.6), 10 days, 40% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3500fold to homogeneity from leaves in an eight-step procedure including ACP affinity chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
native enzyme 147fold from leaves by ammonium sulfate fractionation, ion exchange chromatography, hydrophobic interaction chromatography on a butyl resin, and affinity chromatography, recombinant GST-fusion enzyme from Escherichia coli by glutathione affinity chromatography, GST is cleaved off by thrombin
Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex 200 gel filtration
Q-Sepharose, MonoQ, and hydroxyapatite column chromatographies (native enzyme) or Ni-NTA agarose column chromatography (selenomethionine-substituted enzyme)
recombinant enzyme from strain JT2038 by ammonium sulfate fractionation, gel filtration, and affinity chromatography
recombinant enzyme from Streptomyces lividans by ammonium sulfate fractionation, gel filtration, ion exchange and hydrophobic interaction chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and anion exchange chromatography, followed by ultrafiltration
B1XPH5
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged enzyme from Mycobacterium bovis strain BCG
-
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography and gel filtration, the tag is cleaved off by thrombin
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from strain C41(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant FabHs from Mycobacterium bovis strain BCG by nickel affinity chromatography
recombinant His2-tagged enzyme from Escherichia coli by nickel and Blue Sepharose affinity chromatography, and gel filtration
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinty chromatography, tag cleavage by TEV protease, gel filtration, and ultrafiltration to over 90% purity
recombinant N-terminally His6-tagged FabH from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant native and selenomethionine-labeled enzyme from Escherichia coli strain DH10B to homogeneity by two different steps of anion exchange and a step of hydroxyapatite chromatography
recombinant selenomethionine-labeled enzyme by ion exchange, hydroxylapatite, and affinity chromatography, and gel filtration
-
to homogeneity in three chromatographic steps (Q-Sepharose, MonoQ, and hydroxyapatite)
-
to homogeneity in three chromatographic steps (Q-Sepharose, MonoQ, and hydroxyapatite), immobilized metal ion affinity chromatography (Ni2+)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
codon optimized gene expressed in Lactococcus lactis CL112 (fabH knockout strain)
DNA and amino acid sequence determination and analysis, phylogenetic tree, expression as GST-fusion enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strains DH10B (native enzyme) and BL21(DE3) (selenomethionine-substituted enzyme)
expressed in Ralstonia solanacearum fabH mutant RsmH
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expression of the enzyme in transgenic Nicotiana tabacum using the Agrobacterium tumefaciens transfection system
expression of the native and the selenomethionine-labeled enzyme in Escherichia coli strain DH10B
expression of wild-type and mutant enzymes in strain JM109, coexpression with gene phaC from Aeromonas caviae and gene phaC1 from Pseudomonas sp. strain 61-3
-
gene fabH is transcribed in a gene cluster to produce a leaderless mRNA transcript, transcription analysis, genetic organization, overview
gene fabH or Xoo4209, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene fabH, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
gene fabH, expression of His-tagged enzyme containing a thrombin cleavage site in strain BL21(DE3)
gene fabH, expression of His-tagged wild-type and mutant enzymes in strain BL21(DE3)
-
gene fabH, gene is located on the chromosome, DNA and amino acid sequence determination and analysis, functional complementation of enzyme-defective fabH1 mutant strain CDM5, expression in strain JT2038 alters the endogenous fatty acid composition
gene fabH, overexpression of His-tagged enzyme in Mycobacterium bovis strain BCG
-
gene fabH, overexpression of His-tagged wild-type and mutant FabHs in Mycobacterium bovis strain BCG
gene fabH, overexpression of N-terminal His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene fabH, overexpression of N-terminally His6-tagged FabH in Escherichia coli strain BL21(DE3)
gene fabH, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
B1XPH5
gene fabH, recombinant expression of N-terminally His6-tagged enzyme with a TEV protease cleavage site in Escherichia coli strain BL21(DE3) pLysS
gene fabH, recombinant His-tagged enzyme expression in Escherichia coli strain BL21(DE3)
His-tagged protein expressed in Escherichia coli BL21(DE3)
isozyme KAS3a, DNA and amino acid sequence analysis, expression of KAS3a in Escherichia coli strain K27
isozyme KAS3b, DNA and amino acid sequence analysis, expression of KAS3b in Escherichia coli strain K27
isozymes KAS III-1 and KAS III-2, DNA and amino acid sequence determination and analysis, seed-specific expression of the isozymes in transgenic Nicotiana tabacum, Brassica napus, and Arabidopsis thaliana using a napin gene promoter and the Agrobacterium tumefaciens transfection system
-
overexpressed in E. coli DH10B cells using the pET30 vector, selenomethionine-substituted protein expressed in Escherichia coli BL21(DE3)
-
overexpressed in Escherichia coli DH10B cells using the pET30 vector, selenomethionine-substituted protein expressed in Escherichia coli BL21(DE3)
-
overexpression in strain JM101 inhibits bacterial cell growth and alters the membrane fatty acid composition, overexpression of the chimeric enzyme possessing a transit peptide in Brassica napus seeds and cotyledons via Agrobacterium transfection
-
overexpression of His-tagged wild-type and mutant enzymes in strain C41(DE3)
plastid targeting sequence (first 59 residues) replaced by a His-tag, expressed in Escherichia coli XL1-Blue
seed-specific expression of the isozymes in transgenic Nicotiana tabacum, Brassica napus, and Arabidopsis thaliana using a napin gene promoter and the Agrobacterium tumefaciens transfection system
-
subcloning in Escherichia coli strain TG-2, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform FabH2 is cold-inducible and shows about 2fold increase of expression after cold-shock (8C) treatment
isoform FabH2 is cold-inducible and shows about 2fold increase of expression after cold-shock (8C) treatment
-
isoform FabH2 is cold-inducible and shows about 2fold increase of expression after cold-shock (8C) treatment
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
-
the enzyme is interesting in order to develop engineered high oil-yielding microalgal strains for biofuel production
drug development
medicine
-
the enzyme is a target of antibacterial treatment of the pathogen Staphylococcus aureus
pharmacology
synthesis
-
the recombinant enzyme is useful for production of fatty acids by directed biosynthesis profiting of the flexible substrate specificity for acyl-CoAs of the enzyme, overview
drug development
-
the enzyme represents a target for structure-based design of antimycobacterial agents
drug development
-
the highly conserved enzyme is an attractive target for antimicrobial inhibitor design
drug development
FabH is an attractive target for the development of antibacterial agents
drug development
the enzyme is a target for inhibitor development
drug development
-
FabH is a particularly attractive target for design of antibacterial agents since it is central to the initiation of fatty acid biosynthesis and is highly conserved among Gram positive and negative bacteria
drug development
beta-ketoacyl-ACP-synthase III (FabH or KAS III) has become an attractive target for the development of antibacterial agents which can overcome the multidrug resistance
drug development
the enzyme is a promising target for the development of therapeutic agents
drug development
the enzyme is a promising target for the development of therapeutic agents
drug development
the enzyme is a promising target for the development of therapeutic agents
drug development
-
the enzyme is a promising target for the development of therapeutic agents
drug development
the enzyme is a promising target for the development of therapeutic agents
drug development
the enzyme is a potential target for anti-infection drug discovery, the dimer interface in FabH is potentially a viable target for designing another class of inhibitors
drug development
-
the enzyme is a promising target for the development of therapeutic agents
-
drug development
-
the enzyme is a target for inhibitor development
-
drug development
-
beta-ketoacyl-ACP-synthase III (FabH or KAS III) has become an attractive target for the development of antibacterial agents which can overcome the multidrug resistance
-
drug development
-
the enzyme is a promising target for the development of therapeutic agents
-
pharmacology
-
the enzyme is a target for development of antibiotics
pharmacology
the enzyme is a target for design and development of antibacterial drugs against pathogenic bacteria
pharmacology
-
the enzyme is a target for development of inhibitors for treatment of the multi-drug resistant pathogen Staphylococcus aureus
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clough, R.; Matthis, A.L.; Barnum, S.R.; Jaworski, J.G.
Purification and characterization of 3-ketoacyl-acyl carrier protein synthase III from spinach. A condensing enzyme utilizing acetyl-coenzyme A to initiate fatty acid synthesis
J. Biol. Chem.
267
20992-20998
1992
Spinacia oleracea
brenda
Verwoert, I.I.G.S.; van der Linden, K.H.; Walsh, M.C.; Nijkamp, H.J.J.; Stuitje, A.R.
Modification of Brassica napus seed oil by expression of the Escherichia coli fabH gene, encoding 3-ketoacyl-acyl carrier protein synthase III
Plant Mol. Biol.
27
875-886
1995
Escherichia coli
brenda
Han, L.; Lobo, S.; Reynolds, K.A.
Characterization of beta-ketoacyl-acyl carrier protein synthase III from Streptomyces glaucescens and its role in initiation of fatty acid biosynthesis
J. Bacteriol.
180
4481-4486
1998
Streptomyces glaucescens
brenda
Bao, W.; Sheldon, P.J.; Hutchinson, C.R.
Purification and properties of the Streptomyces peucetius DpsC beta-ketoacyl:acyl carrier protein synthase III that specifies the propionate-starter unit for type II polyketide biosynthesis
Biochemistry
38
9752-9757
1999
Streptomyces peucetius
brenda
Choi, K.H.; Heath, R.J.; Rock, C.O.
beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis
J. Bacteriol.
182
365-370
2000
Bacillus subtilis (O34746), Bacillus subtilis (O07600), Bacillus subtilis, Bacillus subtilis 168 (O07600), Bacillus subtilis 168 (O34746)
brenda
Smirnova, N.; Reynolds, K.A.
Engineered fatty acid biosynthesis in Streptomyces by altered catalytic function of beta-ketoacyl-acyl carrier protein synthase III
J. Bacteriol.
183
2335-2342
2001
Streptomyces glaucescens
brenda
Khandekar, S.S.; Gentry, D.R.; Van Aller, G.S.; Warren, P.; Xiang, H.; Silverman, C.; Doyle, M.L.; Chambers, P.A.; Konstantinidis, A.K.; Brandt, M.; Daines, R.A.; Lonsdale, J.T.
Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)
J. Biol. Chem.
276
30024-30030
2001
Streptococcus pneumoniae (P0A3C5), Streptococcus pneumoniae
brenda
He, X.; Reynolds, K.A.
Purification, characterization, and identification of novel inhibitors of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus
Antimicrob. Agents Chemother.
46
1310-1318
2002
Staphylococcus aureus
brenda
Lai, C.Y.; Cronan, J.E.
beta-Ketoacyl-acyl carrier protein synthase III (FabH) is essential for bacterial fatty acid synthesis
J. Biol. Chem.
278
51494-51503
2003
Lactococcus lactis ssp. lactis, Escherichia coli, Lactococcus lactis ssp. lactis IL1403
brenda
Brown, A.K.; Sridharan, S.; Kremer, L.; Lindenberg, S.; Dover, L.G.; Sacchettini, J.C.; Besra, G.S.
Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-ACP synthase III mtFabH: Factors influencing catalysis and substrate specificity
J. Biol. Chem.
280
32539-32547
2005
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Musayev, F.; Sachdeva, S.; Scarsdale, J.N.; Reynolds, K.A.; Wright, H.T.
Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A
J. Mol. Biol.
346
1313-1321
2005
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Qiu, X.; Choudhry, A.E.; Janson, C.A.; Grooms, M.; Daines, R.A.; Lonsdale, J.T.; Khandekar, S.S.
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus
Protein Sci.
14
2087-2094
2005
Staphylococcus aureus
brenda
Janson, C.A.; Konstantinidis, A.K.; Lonsdale, J.T.; Qiu, X.
Crystallization of Escherichia coli beta-ketoacyl-ACP synthase III and the use of a dry flash-cooling technique for data collection
Acta Crystallogr. Sect. D
56
747-748
2000
Escherichia coli
brenda
He, X.; Reeve, A.M.; Desai, U.R.; Kellogg, G.E.; Reynolds, K.A.
1,2-dithiole-3-ones as potent inhibitors of the bacterial 3-ketoacyl acyl carrier protein synthase III (FabH)
Antimicrob. Agents Chemother.
48
3093-3102
2004
Escherichia coli (P0A6R0), Escherichia coli, Staphylococcus aureus
brenda
Kiatpapan, P.; Kobayashi, H.; Sakaguchi, M.; Ono, H.; Yamashita, M.; Kaneko, Y.; Murooka, Y.
Molecular characterization of Lactobacillus plantarum genes for beta-ketoacyl-acyl carrier protein synthase III (fabH) and acetyl coenzyme A carboxylase (accBCDA), which are essential for fatty acid biosynthesis
Appl. Environ. Microbiol.
67
426-433
2001
Lactiplantibacillus plantarum (Q88YZ4), Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC BAA-793 (Q88YZ4)
brenda
Nomura, C.T.; Taguchi, K.; Taguchi, S.; Doi, Y.
Coexpression of genetically engineered 3-ketoacyl-ACP synthase III (fabH) and polyhydroxyalkanoate synthase (phaC) genes leads to short-chain-length-medium-chain-length polyhydroxyalkanoate copolymer production from glucose in Escherichia coli JM109
Appl. Environ. Microbiol.
70
999-1007
2004
Escherichia coli
brenda
Khandekar, S.S.; Konstantinidis, A.K.; Silverman, C.; Janson, C.A.; McNulty, D.E.; Nwagwu, S.; Van Aller, G.S.; Doyle, M.L.; Kane, J.F.; Qiu, X.; Lonsdale, J.
Expression, purification, and crystallization of the Escherichia coli selenomethionyl beta-ketoacyl-acyl carrier protein synthase III
Biochem. Biophys. Res. Commun.
270
100-107
2000
Escherichia coli
brenda
Abbadi, A.; Brummel, M.; Schutt, B.S.; Slabaugh, M.B.; Schuch, R.; Spener, F.
Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme
Biochem. J.
345
153-160
2000
Cuphea wrightii
brenda
Florova, G.; Kazanina, G.; Reynolds, K.A.
Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity
Biochemistry
41
10462-10471
2002
Streptomyces glaucescens
brenda
Revill, W.P.; Bibb, M.J.; Scheu, A.K.; Kieser, H.J.; Hopwood, D.A.
beta-Ketoacyl acyl carrier protein synthase III (FabH) is essential for fatty acid biosynthesis in Streptomyces coelicolor A3(2)
J. Bacteriol.
183
3526-3530
2001
Streptomyces coelicolor (P72392), Streptomyces coelicolor
brenda
Li, Y.; Florova, G.; Reynolds, K.A.
Alteration of the fatty acid profile of Streptomyces coelicolor by replacement of the initiation enzyme 3-ketoacyl acyl carrier protein synthase III (FabH)
J. Bacteriol.
187
3795-3799
2005
Streptomyces coelicolor
brenda
Tsay, J.T.; Oh, W.; Larson, T.J.; Jackowski, S.; Rock, C.O.
Isolation and characterization of the beta-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12
J. Biol. Chem.
267
6807-6814
1992
Escherichia coli K-12 (P0A6R0), Escherichia coli K-12
brenda
Heath, R.J.; Rock, C.O.
Inhibition of beta-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli
J. Biol. Chem.
271
10996-11000
1996
Escherichia coli
brenda
Qiu, X.; Janson, C.A.; Konstantinidis, A.K.; Nwagwu, S.; Silverman, C.; Smith, W.W.; Khandekar, S.; Lonsdale, J.; Abdel-Meguid, S.S.
Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis
J. Biol. Chem.
274
36465-36471
1999
Escherichia coli
brenda
Choi, K.H.; Kremer, L.; Besra, G.S.; Rock, C.O.
Identification and substrate specificity of beta-ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis
J. Biol. Chem.
275
28201-28207
2000
Mycobacterium tuberculosis
brenda
Scarsdale, J.N.; Kazanina, G.; He, X.; Reynolds, K.A.; Wright, H.T.
Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III
J. Biol. Chem.
276
20516-20522
2001
Mycobacterium tuberculosis
brenda
Nie, Z.; Perretta, C.; Lu, J.; Su, Y.; Margosiak, S.; Gajiwala, K.S.; Cortez, J.; Nikulin, V.; Yager, K.M.; Appelt, K.; Chu, S.
Structure-based design, synthesis, and study of potent inhibitors of beta-ketoacyl-acyl carrier protein synthase III as potential antimicrobial agents
J. Med. Chem.
48
1596-1609
2005
Enterococcus faecalis
brenda
Qiu, X.; Janson, C.A.; Smith, W.W.; Head, M.; Lonsdale, J.; Konstantinidis, A.K.
Refined structures of beta-ketoacyl-acyl carrier protein synthase III
J. Mol. Biol.
307
341-356
2001
Escherichia coli (P0A6R0), Escherichia coli
brenda
Hwang, S.K.; Hwang, Y.S.
Molecular cloning and functional expression of Perilla frutescens 3-ketoacyl-(acyl carrier protein) synthase III
Mol. Cells
10
375-381
2000
Perilla frutescens (O48945), Perilla frutescens (O48944), Perilla frutescens
brenda
Abbadi, A.; Brummel, M.; Spener, F.
Knockout of the regulatory site of 3-ketoacyl-ACP synthase III enhances short- and medium-chain acyl-ACP synthesis
Plant J.
24
1-9
2000
Cuphea wrightii (P49244), Cuphea wrightii (P49245), Cuphea wrightii
brenda
Dehesh, K.; Tai, H.; Edwards, P.; Byrne, J.; Jaworski, J.G.
Overexpression of 3-ketoacyl-acyl-carrier protein synthase IIIs in plants reduces the rate of lipid synthesis
Plant Physiol.
125
1103-1114
2001
Brassica napus, Cuphea hookeriana, Nicotiana tabacum, Spinacia oleracea (Q07510), Spinacia oleracea
brenda
Brueck, F.M.; Brummel, M.; Schuch, R.; Spener, F.
In-vitro evidence for feed-back regulation of beta-ketoacyl-acyl carrier protein synthase III in medium-chain fatty acid biosynthesis
Planta
198
271-278
1996
Cuphea lanceolata
-
brenda
Jones, A.L.; Gane, A.M.; Herbert, D.; Willey, D.L.; Rutter, A.J.; Kille, P.; Dancer, J.E.; Harwood, J.L.
beta-Ketoacyl-acyl carrier protein synthase III from pea (Pisum sativum L.): properties, inhibition by a novel thiolactomycin analogue and isolation of a cDNA clone encoding the enzyme
Planta
216
752-761
2003
Lathyrus oleraceus (Q9FSD6)
brenda
Davies, C.; Heath, R.J.; White, S.W.; Rock, C.O.
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli
Structure
8
185-195
2000
Escherichia coli
brenda
Alhamadsheh, M.M.; Waters, N.C.; Huddler, D.P.; Kreishman-Deitrick, M.; Florova, G.; Reynolds, K.A.
Synthesis and biological evaluation of thiazolidine-2-one 1,1-dioxide as inhibitors of Escherichia coli beta-ketoacyl-ACP-synthase III (FabH)
Bioorg. Med. Chem. Lett.
17
879-883
2007
Escherichia coli (P0A6R0), Escherichia coli, Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG3), Plasmodium falciparum, Plasmodium falciparum D6
brenda
Wang, J.; Kodali, S.; Lee, S.H.; Galgoci, A.; Painter, R.; Dorso, K.; Racine, F.; Motyl, M.; Hernandez, L.; Tinney, E.; Colletti, S.L.; Herath, K.; Cummings, R.; Salazar, O.; Gonzalez, I.; Basilio, A.; Vicente, F.; Genilloud, O.; Pelaez, F.; Jayasuriya, H.; Young, K.; Cully, D.F.; Singh, S.B.
Discovery of platencin, a dual FabF and FabH inhibitor with in vivo antibiotic properties
Proc. Natl. Acad. Sci. USA
104
7612-7616
2007
Staphylococcus aureus
brenda
Sachdeva, S.; Musayev, F.; Alhamadsheh, M.M.; Neel Scarsdale, J.; Tonie Wright, H.; Reynolds, K.A.
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates
Bioorg. Chem.
36
85-90
2008
Mycobacterium tuberculosis
brenda
Jeong, K.; Lee, J.; Kim, Y.
Homology modeling and docking study of beta-ketoacyl acyl carrier protein synthase III from Enterococcus faecalis
Bull. Korean Chem. Soc.
28
1335-1340
2007
Enterococcus faecalis
-
brenda
Alhamadsheh, M.M.; Musayev, F.; Komissarov, A.A.; Sachdeva, S.; Wright, H.T.; Scarsdale, N.; Florova, G.; Reynolds, K.A.
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes
Chem. Biol.
14
513-524
2007
Escherichia coli, Mycobacterium tuberculosis
brenda
Sachdeva, S.; Musayev, F.N.; Alhamadsheh, M.M.; Scarsdale, J.N.; Wright, H.T.; Reynolds, K.A.
Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH
Chem. Biol.
15
402-412
2008
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Ashek, A.; San Juan, A.A.; Cho, S.J.
HQSAR study of beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitors
J. Enzyme Inhib. Med. Chem.
22
7-14
2007
Enterococcus faecalis
brenda
Sachdeva, S.; Reynolds, K.A.
Mycobacterium tuberculosis beta-ketoacyl acyl carrier protein synthase III (mtFabH) assay: principles and method
Methods Mol. Med.
142
205-213
2008
Mycobacterium tuberculosis
brenda
Castillo, Y.P.; Perez, M.A.
Bacterial beta-ketoacyl-acyl carrier protein synthase III (FabH): an attractive target for the design of new broad-spectrum antimicrobial agents
Mini Rev. Med. Chem.
8
36-45
2008
Escherichia coli, Staphylococcus aureus, Mycobacterium tuberculosis, Enterococcus faecium, Streptococcus pneumoniae, Pseudomonas aeruginosa, Neisseria meningitidis, Haemophilus influenzae, Streptococcus pyogenes
brenda
Li, J.; Li, M.; Wu, P.; Tian, C.; Jiang, H.; Wu, G.
Molecular cloning and expression analysis of a gene encoding a putative beta-ketoacyl-acyl carrier protein (ACP) synthase III (KAS III) from Jatropha curcas
Tree Physiol.
28
921-927
2008
Jatropha curcas
brenda
Huynh, K.H.; Natarajan, S.; Song, N.H.; Ngo, P.T.; Ahn, Y.J.; Kim, J.G.; Lee, B.M.; Eo, Y.D.; Kang, L.W.
Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of beta-ketoacyl-ACP synthase III (FabH) from Xanthomonas oryzae pv. oryzae
Acta Crystallogr. Sect. F
65
460-462
2009
Xanthomonas oryzae pv. oryzae, Xanthomonas oryzae pv. oryzae Xoo KACC10331
brenda
Matsumoto, K.; Murata, T.; Nagao, R.; Nomura, C.T.; Arai, S.; Arai, Y.; Takase, K.; Nakashita, H.; Taguchi, S.; Shimada, H.
Production of short-chain-length/medium-chain-length polyhydroxyalkanoate (PHA) copolymer in the plastid of Arabidopsis thaliana using an engineered 3-ketoacyl-acyl carrier protein synthase III
Biomacromolecules
10
686-690
2009
Arabidopsis thaliana, Escherichia coli
brenda
Lv, P.C.; Wang, K.R.; Yang, Y.; Mao, W.J.; Chen, J.; Xiong, J.; Zhu, H.L.
Design, synthesis and biological evaluation of novel thiazole derivatives as potent FabH inhibitors
Bioorg. Med. Chem. Lett.
19
6750-6754
2009
Escherichia coli
brenda
Lee, J.Y.; Jeong, K.W.; Lee, J.U.; Kang, D.I.; Kim, Y.
Novel E. coli beta-ketoacyl-acyl carrier protein synthase III inhibitors as targeted antibiotics
Bioorg. Med. Chem.
17
1506-1513
2009
Escherichia coli K-12
brenda
Lee, J.Y.; Jeong, K.W.; Shin, S.; Lee, J.U.; Kim, Y.
Antimicrobial natural products as beta-ketoacyl-acyl carrier protein synthase III inhibitors
Bioorg. Med. Chem.
17
5408-5413
2009
Escherichia coli K-12
brenda
Li, H.Q.; Shi, L.; Li, Q.S.; Liu, P.G.; Luo, Y.; Zhao, J.; Zhu, H.L.
Synthesis of C(7) modified chrysin derivatives designing to inhibit beta-ketoacyl-acyl carrier protein synthase III (FabH) as antibiotics
Bioorg. Med. Chem.
17
6264-6269
2009
Escherichia coli (P0A6R0), Escherichia coli
brenda
Singh, S.; Soni, L.; Gupta, M.; Prabhakar, Y.; Kaskhedikar, S.
QSAR studies on benzoylaminobenzoic acid derivatives as inhibitors of beta-ketoacyl-acyl carrier protein synthase III
Eur. J. Med. Chem.
43
1071-1080
2008
Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Enterococcus faecalis, Neisseria meningitidis, Escherichia coli
brenda
Singh, A.K.; Zhang, Y.M.; Zhu, K.; Subramanian, C.; Li, Z.; Jayaswal, R.K.; Gatto, C.; Rock, C.O.; Wilkinson, B.J.
FabH selectivity for anteiso branched-chain fatty acid precursors in low-temperature adaptation in Listeria monocytogenes
FEMS Microbiol. Lett.
301
188-192
2009
Listeria monocytogenes (C0LNR0), Listeria monocytogenes, Listeria monocytogenes 10403S (C0LNR0)
brenda
Veyron-Churlet, R.; Molle, V.; Taylor, R.C.; Brown, A.K.; Besra, G.S.; Zanella-Cleon, I.; Fuetterer, K.; Kremer, L.
The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue
J. Biol. Chem.
284
6414-6424
2009
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Lee, P.J.; Bhonsle, J.B.; Gaona, H.W.; Huddler, D.P.; Heady, T.N.; Kreishman-Deitrick, M.; Bhattacharjee, A.; McCalmont, W.F.; Gerena, L.; Lopez-Sanchez, M.; Roncal, N.E.; Hudson, T.H.; Johnson, J.D.; Prigge, S.T.; Waters, N.C.
Targeting the fatty acid biosynthesis enzyme, beta-ketoacyl-acyl carrier protein synthase III (PfKASIII), in the identification of novel antimalarial agents
J. Med. Chem.
52
952-963
2009
Plasmodium falciparum
brenda
Al-Balas, Q.; Anthony, N.G.; Al-Jaidi, B.; Alnimr, A.; Abbott, G.; Brown, A.K.; Taylor, R.C.; Besra, G.S.; McHugh, T.D.; Gillespie, S.H.; Johnston, B.F.; Mackay, S.P.; Coxon, G.D.
Identification of 2-aminothiazole-4-carboxylate derivatives active against Mycobacterium tuberculosis H37Rv and the beta-ketoacyl-ACP synthase mtFabH
PLoS ONE
4
e5617
2009
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Wen, L.; Chmielowski, J.N.; Bohn, K.C.; Huang, J.K.; Timsina, Y.N.; Kodali, P.; Pathak, A.K.
Functional expression of Francisella tularensis FabH and FabI, potential antibacterial targets
Protein Expr. Purif.
65
83-91
2009
Francisella tularensis subsp. holarctica (A0SPA8)
brenda
Pereira, J.H.; Goh, E.B.; Keasling, J.D.; Beller, H.R.; Adams, P.D.
Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus
Acta Crystallogr. Sect. D
68
1320-1328
2012
Micrococcus luteus (C5CAR9)
brenda
Du, Y.; Gisselberg, J.E.; Johnson, J.D.; Lee, P.J.; Prigge, S.T.; Bachmann, B.O.
Lactococcus lactis fabH, encoding beta-ketoacyl-acyl carrier protein synthase, can be functionally replaced by the Plasmodium falciparum congener
Appl. Environ. Microbiol.
76
3959-3966
2010
Plasmodium falciparum (O77078), Plasmodium falciparum, Lactococcus lactis (Q9CHG0), Lactococcus lactis, Lactococcus lactis IL1403 (Q9CHG0)
brenda
Lv, P.C.; Sun, J.; Luo, Y.; Yang, Y.; Zhu, H.L.
Design, synthesis, and structure-activity relationships of pyrazole derivatives as potential FabH inhibitors
Bioorg. Med. Chem. Lett.
20
4657-4660
2010
Escherichia coli
brenda
Yang, Y.S.; Zhang, F.; Gao, C.; Zhang, Y.B.; Wang, X.L.; Tang, J.F.; Sun, J.; Gong, H.B.; Zhu, H.L.
Discovery and modification of sulfur-containing heterocyclic pyrazoline derivatives as potential novel class of beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitors
Bioorg. Med. Chem. Lett.
22
4619-4624
2012
Escherichia coli
brenda
Li, Z.L.; Li, Q.S.; Zhang, H.J.; Hu, Y.; Zhu, D.D.; Zhu, H.L.
Design, synthesis and biological evaluation of urea derivatives from o-hydroxybenzylamines and phenylisocyanate as potential FabH inhibitors
Bioorg. Med. Chem.
19
4413-4420
2011
Escherichia coli
brenda
Li, H.Q.; Luo, Y.; Zhu, H.L.
Discovery of vinylogous carbamates as a novel class of beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitors
Bioorg. Med. Chem.
19
4454-4459
2011
Escherichia coli
brenda
Zhang, H.J.; Zhu, D.D.; Li, Z.L.; Sun, J.; Zhu, H.L.
Synthesis, molecular modeling and biological evaluation of beta-ketoacyl-acyl carrier protein synthase III (FabH) as novel antibacterial agents
Bioorg. Med. Chem.
19
4513-4519
2011
Escherichia coli
brenda
Li, Y.; Luo, Y.; Hu, Y.; Zhu, D.D.; Zhang, S.; Liu, Z.J.; Gong, H.B.; Zhu, H.L.
Design, synthesis and antimicrobial activities of nitroimidazole derivatives containing 1,3,4-oxadiazole scaffold as FabH inhibitors
Bioorg. Med. Chem.
20
4316-4322
2012
Escherichia coli
brenda
Mueller, A.P.; Nomura, C.T.
Mutations to the active site of 3-ketoacyl-ACP synthase III (FabH) increase polyhydroxyalkanoate biosynthesis in transgenic Escherichia coli
J. Biosci. Bioeng.
113
300-306
2012
Escherichia coli
brenda
Gonzalez-Mellado, D.; von Wettstein-Knowles, P.; Garces, R.; Martinez-Force, E.
The role of beta-ketoacyl-acyl carrier protein synthase III in the condensation steps of fatty acid biosynthesis in sunflower
Planta
231
1277-1289
2010
Helianthus annuus (A5A0S1), Helianthus annuus CAS-6 (A5A0S1)
brenda
Cheng, K.; Xue, J.Y.; Zhu, H.L.
Design, synthesis and antibacterial activity studies of thiazole derivatives as potent ecKAS III inhibitors
Bioorg. Med. Chem. Lett.
23
4235-4238
2013
Escherichia coli (P0A6R0), Escherichia coli
brenda
Song, X.; Yang, Y.; Zhao, J.; Chen, Y.
Synthesis and antibacterial activity of cinnamaldehyde acylhydrazone with a 1,4-benzodioxan fragment as a novel class of potent beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitor
Chem. Pharm. Bull.
62
1110-1118
2014
Escherichia coli (P0A6R0), Pseudomonas aeruginosa (Q9HYR2), Staphylococcus aureus, Bacillus subtilis (O07600), Bacillus subtilis 168 (O07600), Staphylococcus aureus ATCC 6538
brenda
Wang, Y.; Ma, S.
Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents
ChemMedChem
8
1589-1608
2013
Bacillus subtilis (O34746), Escherichia coli (P0A6R0), Haemophilus influenzae (P43711), Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis H37Rv (P9WNG3), Pseudomonas aeruginosa (A0A072ZQE7), Staphylococcus aureus (P99159), Staphylococcus aureus N315 (P99159), Streptococcus pneumoniae (P0A3C5)
brenda
Li, J.R.; Li, D.D.; Wang, R.R.; Sun, J.; Dong, J.J.; Du, Q.R.; Fang, F.; Zhang, W.M.; Zhu, H.L.
Design and synthesis of thiazole derivatives as potent FabH inhibitors with antibacterial activity
Eur. J. Med. Chem.
75
438-447
2014
Escherichia coli (P0A6R0)
brenda
Misra, N.; Patra, M.; Panda, P.; Sukla, L.; Mishra, B.
Homology modeling and docking studies of FabH (beta-ketoacyl-ACP synthase III) enzyme involved in type II fatty acid biosynthesis of Chlorella variabilis: a potential algal feedstock for biofuel production
J. Biomol. Struct. Dyn.
31
241-257
2013
Chlorella variabilis
brenda
Ramamoorthy, D.; Turos, E.; Guida, W.C.
Identification of a new binding site in E. coli FabH using molecular dynamics simulations: validation by computational alanine mutagenesis and docking studies
J. Chem. Inf. Model.
53
1138-1156
2013
Escherichia coli (P0A6R0)
brenda
Mittal, A.; Johnson, M.E.
Conformational diversity of bacterial FabH: implications for molecular recognition specificity
J. Mol. Graph. Model.
55
115-122
2015
Escherichia coli (P0A6R0), Enterococcus faecalis (Q820T1), Enterococcus faecalis ATCC 700802 (Q820T1)
brenda
Shamim, A.; Abbasi, S.W.; Azam, S.S.
Structural and dynamical aspects of Streptococcus gordonii FabH through molecular docking and MD simulations
J. Mol. Graph. Model.
60
180-196
2015
Streptococcus gordonii (A8AYW5), Streptococcus gordonii ATCC 35105 (A8AYW5)
brenda
Kuo, J.; Khosla, C.
The initiation ketosynthase (FabH) is the sole rate-limiting enzyme of the fatty acid synthase of Synechococcus sp. PCC 7002
Metab. Eng.
22
53-59
2014
Synechococcus sp. (B1XPH5), Synechococcus sp., Synechococcus sp. PCC 7002 (B1XPH5)
brenda
Nanson, J.D.; Himiari, Z.; Swarbrick, C.M.; Forwood, J.K.
Structural characterisation of the beta-ketoacyl-acyl carrier protein synthases, FabF and FabH, of Yersinia pestis
Sci. Rep.
5
14797
2015
Yersinia pestis (Q8ZFT7)
brenda
Abugrain, M.E.; Brumsted, C.J.; Osborn, A.R.; Philmus, B.; Mahmud, T.
A highly promiscuous beta-ketoacyl-ACP synthase (KAS) III-like protein is involved in pactamycin biosynthesis
ACS Chem. Biol.
12
362-366
2017
Streptomyces pactum
brenda
Meng, Q.; Liang, H.; Gao, H.
Roles of multiple KASIII homologues of Shewanella oneidensis in initiation of fatty acid synthesis and in cerulenin resistance
Biochim. Biophys. Acta
1863
1153-1163
2018
Shewanella oneidensis, Shewanella oneidensis ATCC 700550
brenda
Zhou, Y.; Yang, Y.S.; Song, X.D.; Lu, L.; Zhu, H.L.
Study of Schiff-base-derived with dioxygenated rings and nitrogen heterocycle as potential beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitors
Chem. Pharm. Bull.
65
178-185
2017
Escherichia coli (P0A6R0)
brenda
Patil, K.; Wakkar, L.; Undare, S.; Kolekar, G.; Deshmukh, M.; Choudhari, P.; Anbhule, P.
Selective synthesis of 10,11-dihydrochromeno[4,3-b]chromene-6,8(7H,9H)-dione using copper oxide nanoparticles for potential inhibitors of beta-ketoacyl-[acyl-carrier-protein] synthase III of Mycobacterium tuberculosis
Indian J. Chem.
55B
1151-1159
2016
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
-
brenda
Zhang, D.; Zhang, F.; Liu, W.
A KAS-III heterodimer in lipstatin biosynthesis nondecarboxylatively condenses C8 and C14 fatty acyl-CoA substrates by a variable mechanism during the establishment of a C22 aliphatic skeleton
J. Am. Chem. Soc.
141
3993-4001
2019
Streptomyces toxytricini
brenda
Cao, W.; Ma, W.; Zhang, B.; Wang, X.; Chen, K.; Li, Y.; Ouyang, P.
Improved pinocembrin production in Escherichia coli by engineering fatty acid synthesis
J. Ind. Microbiol. Biotechnol.
43
557-566
2016
Escherichia coli (P0A6R0)
brenda
Nofiani, R.; Philmus, B.; Nindita, Y.; Mahmud, T.
3-Ketoacyl-ACP synthase (KAS) III homologues and their roles in natural product biosynthesis
MedChemComm
10
1517-1530
2019
Actinacidiphila reveromycinica, Actinomadura kijaniata, Actinomadura kijaniata SCC1256, Corallococcus coralloides, Corallococcus coralloides B035, Dactylosporangium aurantiacum subsp. hamdenensis, Dactylosporangium aurantiacum subsp. hamdenensis NRRL 18085, Escherichia coli (P0A6R0), Micromonospora carbonacea, Micromonospora echinospora, Micromonospora echinospora NRRL 15839, Micromonospora maris, Micromonospora maris AB-18-032, Myxococcus fulvus, Myxococcus fulvus Mxf50, Paractinoplanes deccanensis, Polymorphospora rubra, Polymorphospora rubra K07-0510, Pseudomonas aeruginosa (Q9HYR2), Pseudomonas chlororaphis subsp. aurantiaca, Pseudomonas chlororaphis subsp. aurantiaca BL915, Pseudomonas putida, Pseudomonas putida BW11M1, Streptomyces albus, Streptomyces albus XM211, Streptomyces antibioticus, Streptomyces antibioticus DSM 4072, Streptomyces antibioticus Tue2706, Streptomyces coelicolor, Streptomyces coelicolor M511, Streptomyces galilaeus, Streptomyces galilaeus 3AR-33, Streptomyces griseoruber, Streptomyces griseus, Streptomyces griseus ATCC 49344, Streptomyces nodosus subsp. asukaensis, Streptomyces pactum, Streptomyces pactum ATCC 27456, Streptomyces peucetius, Streptomyces roseofulvus, Streptomyces roseofulvus AM-3867, Streptomyces sp. 88-682, Streptomyces sp. A2991200, Streptomyces sp. CL190, Streptomyces sp. CM020, Streptomyces sp. KCTC 11604BP, Streptomyces sp. MA347, Streptomyces sp. NRRL 11266, Streptomyces sp. NRRL 12068, Streptomyces sp. SF2575, Streptomyces tendae, Streptomyces tendae HKI 017, Streptomyces toxytricini, Streptomyces viridochromogenes, Streptomyces viridochromogenes Tue57
brenda
Lee, W.C.; Jeong, M.C.; Lee, Y.; Kwak, C.; Lee, J.Y.; Kim, Y.
Structure and substrate specificity of beta-ketoacyl-acyl carrier protein synthase III from Acinetobacter baumannii
Mol. Microbiol.
108
567-577
2018
Acinetobacter baumannii
brenda
Yu, Y.; Ma, J.; Miao, X.; Wang, H.
Biological function research of 3-ketoacyl ACP synthase III from different bacteria
Prog. Biochem. Biophys.
43
1004-1012
2016
Bacillus subtilis (O34746 AND O07600), Escherichia coli (P0A6R0), Ralstonia solanacearum, Xanthomonas oryzae pv. oryzae, Staphylococcus aureus, Streptomyces coelicolor, Bacillus subtilis 168 (O34746 AND O07600)
-
brenda
Alhamadsheh, M.; Waters, N.C.; Sachdeva, S.; Lee, P.; Reynolds, K.A.
Synthesis and biological evaluation of novel sulfonyl-naphthalene-1,4-diols as FabH inhibitors
Bioorg. Med. Chem. Lett.
18
6402-6405
2008
Escherichia coli (P0A6R0), Plasmodium falciparum
brenda
Yan, X.; Zhang, J.; Tan, H.; Liu, Z.; Jiang, K.; Tian, W.; Zheng, M.; Lin, Z.; Deng, Z.; Qu, X.
A pair of atypical KAS III homologues with initiation and elongation functions program the polyketide biosynthesis in asukamycin
Angew. Chem. Int. Ed. Engl.
61
e202200879
2022
Escherichia coli
brenda
Guo, Q.; Su, J.; Liao, Y.; Yu, Y.; Luo, L.; Weng, X.; Zhang, W.; Hu, Z.; Wang, H.; Beattie, G.A.; Ma, J.
An atypical 3-ketoacyl ACP synthase III required for acyl homoserine lactone synthesis in Pseudomonas syringae pv. syringae B728a
Appl. Environ. Microbiol.
90
e0225623
2024
Pseudomonas syringae pv. syringae, Pseudomonas syringae pv. syringae B728a
brenda
Ejaz, S.A.; Aziz, M.; Wani, T.A.; Al-Kahtani, H.M.
Evaluation of mechanical features and antibacterial potential of fluoroquinolone against beta-ketoacyl-ACP synthases (FabB, FabF & FabH) via computational approaches
Arch. Biochem. Biophys.
744
109674
2023
Escherichia coli (P0A6R0)
brenda
Sun, J.; Zhang, C.P.; Chen, C.H.; Guo, X.M.; Liu, C.S.; Zhou, Y.; Hu, F.L.
Design, synthesis and molecular docking of 1,3,4-oxadiazole-2(3H)-thione derivatives containing 1,4-benzodioxane skeleton as potential FabH inhibitors
Chem. Biodivers.
20
e202201060
2023
Escherichia coli (P0A6R0)
brenda
Zhou, Y.; Liang, Y.Q.; Wang, X.Y.; Chang, H.Y.; Hu, S.P.; Sun, J.
Design, synthesis and antibacterial activities of novel amide derivatives bearing dioxygenated rings as potential beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitors
Chem. Pharm. Bull. (Tokyo)
70
544-549
2022
Escherichia coli (P0A6R0)
brenda
Zhao, S.; Xiao, C.; Wang, J.; Tian, K.; Ji, W.; Yang, T.; Khan, B.; Qian, G.; Yan, W.; Ye, Y.
Discovery of natural FabH inhibitors using an immobilized enzyme column and their antibacterial activity against Xanthomonas oryzae pv. oryzae
J. Agric. Food Chem.
68
14204
2020
Xanthomonas oryzae pv. oryzae
brenda
Ha, Y.; Jang, M.; Lee, S.; Lee, J.Y.; Lee, W.C.; Bae, S.; Kang, J.; Han, M.; Kim, Y.
Identification of inhibitor binding hotspots in Acinetobacter baumannii beta-ketoacyl acyl carrier protein synthase III using molecular dynamics simulation
J. Mol. Graph. Model.
100
107669
2020
Acinetobacter baumannii (D0CFW5)
brenda
Saeed, A.U.; Rahman, M.U.; Chen, H.F.; Zheng, J.
Structural insight of KSIII (beta-Ketoacyl-ACP synthase)-like acyltransferase ChlB3 in the biosynthesis of chlorothricin
Molecules
27
6405
2022
Streptomyces antibioticus (Q0R4P5), Streptomyces antibioticus DSM-40725 (Q0R4P5)
brenda
Ma, J.R.; Lin, J.Y.; Zhang, Y.Y.; Chen, Y.; Zhang, W.B.; Ni, X.P.; Yu, Y.H.
SCO6564, a novel 3-ketoacyl acyl carrier protein synthase III, contributes in fatty acid synthesis in Streptomyces coelicolor
PLoS ONE
20
e0318258
2025
Streptomyces coelicolor, Streptomyces coelicolor M145
brenda
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