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Enzyme Nomenclature
Information on EC 2.3.1.301 - mycobacterial beta-ketoacyl-[acyl carrier protein] synthase III
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EC Tree
2.3.1.301 mycobacterial beta-ketoacyl-[acyl carrier protein] synthase IIIIUBMB Comments
The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms. The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids. The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, beta-ketoacyl-[acyl-carrier-protein] synthase III, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300, branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase.
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The expected taxonomic range for this enzyme is: Mycobacterium tuberculosis
Reaction Schemes
+
=
a 3-oxotetradecanoyl-[acyl-carrier protein]
+
+
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FabH
mycobacterial 3-oxoacyl-[acyl carrier protein] synthase III
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-
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Rv0533c
FabH
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-
ambiguous, gene name
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dodecanoyl-CoA + a malonyl-[acyl-carrier protein] = a 3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
dodecanoyl-CoA:malonyl-[acyl-carrier protein] C-acyltransferase
The enzyme, characterized from mycobacteria, provides a link between the type I and type II fatty acid synthase systems (FAS-I and FAS-II, respectively) found in these organisms. The enzyme acts on medium- and long-chain acyl-CoAs (C12-C16) produced by the FAS-I system, condensing them with malonyl-[acyl-carrier protein] (malonyl-AcpM) and forming starter molecules for the FAS-II system, which elongates them into meromycolic acids. The enzyme has no activity with short-chain acyl-CoAs (e.g. acetyl-CoA), which are used by EC 2.3.1.180, beta-ketoacyl-[acyl-carrier-protein] synthase III, or branched-chain acyl-CoAs, which are used by EC 2.3.1.300, branched-chain beta-ketoacyl-[acyl-carrier-protein] synthase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
dodecanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxotetradecanoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
myristoyl-CoA + a malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
palmitoyl-CoA + malonyl-[ACP]
3-oxostearoyl-[ACP] + CoA + CO2
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-
-
?
palmitoyl-CoA + malonyl-[acyl-carrier protein]
3-oxostearoyl-[acyl-carrier protein] + CoA + CO2
stearoyl-CoA + malonyl-[ACP]
3-oxoicosanoyl-[ACP] + CoA + CO2
-
-
-
?
tetradecanoyl-CoA + malonyl-[ACP]
3-oxopalmitoyl-[ACP] + CoA + CO2
-
-
-
?
arachoyl-CoA + malonyl-[ACP]
3-oxodocosanoyl-[ACP] + CoA + CO2
-
-
-
?
arachoyl-CoA + malonyl-[ACP]
3-oxodocosanoyl-[ACP] + CoA + CO2
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-
-
?
decanoyl-CoA + malonyl-[ACP]
3-oxododecanoyl-[ACP] + CoA + CO2
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-
-
?
decanoyl-CoA + malonyl-[ACP]
3-oxododecanoyl-[ACP] + CoA + CO2
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-
-
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
dodecanoyl-CoA + malonyl-[ACP]
3-oxotetradecanoyl-[ACP] + CoA + CO2
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-
-
?
dodecanoyl-CoA + malonyl-[ACP]
3-oxotetradecanoyl-[ACP] + CoA + CO2
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-
-
?
hexanoyl-CoA + malonyl-[ACP]
3-oxooctanoyl-[ACP] + CoA + CO2
ACP i.e. Escherichia coli acyl-carrier protein
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-
?
hexanoyl-CoA + malonyl-[ACP]
3-oxooctanoyl-[ACP] + CoA + CO2
ACP i.e. Escherichia coli acyl-carrier protein
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-
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
-
-
-
?
myristoyl-CoA + a malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
myristoyl-CoA + a malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
octanoyl-CoA + malonyl-[AcpM]
3-oxodecanoyl-[ACP] + CoA + CO2
AcpM i.e. natural partner Mycobacterium tuberculosis acyl-carrier protein
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?
octanoyl-CoA + malonyl-[AcpM]
3-oxodecanoyl-[ACP] + CoA + CO2
AcpM i.e. natural partner Mycobacterium tuberculosis acyl-carrier protein
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-
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
-
-
-
?
palmitoyl-CoA + malonyl-[acyl-carrier protein]
3-oxostearoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
palmitoyl-CoA + malonyl-[acyl-carrier protein]
3-oxostearoyl-[acyl-carrier protein] + CoA + CO2
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?
additional information
?
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FabH clearly prefers long-chain acyl-CoA substrates rather than acyl-ACP primers and does not utilize acetyl-CoA as a primer. No substrates: acetyl-CoA, butyryl-CoA, or isovaleryl-CoA
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additional information
?
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enzyme catalyzes a Claisen-type condensation between long chain acyl-CoA substrates such as myristoyl-CoA (C14) and malonyl-ACP. No substrates: acetyl-CoA, butanoyl-CoA
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additional information
?
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FabH clearly prefers long-chain acyl-CoA substrates rather than acyl-ACP primers and does not utilize acetyl-CoA as a primer. No substrates: acetyl-CoA, butyryl-CoA, or isovaleryl-CoA
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additional information
?
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enzyme catalyzes a Claisen-type condensation between long chain acyl-CoA substrates such as myristoyl-CoA (C14) and malonyl-ACP. No substrates: acetyl-CoA, butanoyl-CoA
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[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-oxostearoyl-[acyl-carrier protein] + CoA + CO2
-
-
-
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
-
-
-
?
decanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxolauroyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
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-
?
lauroyl-CoA + malonyl-[acyl-carrier protein]
3-oxomyristoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
myristoyl-CoA + malonyl-[acyl-carrier protein]
3-oxopalmitoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
octanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CoA + CO2
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-
-
?
additional information
?
-
FabH clearly prefers long-chain acyl-CoA substrates rather than acyl-ACP primers and does not utilize acetyl-CoA as a primer. No substrates: acetyl-CoA, butyryl-CoA, or isovaleryl-CoA
-
-
-
additional information
?
-
FabH clearly prefers long-chain acyl-CoA substrates rather than acyl-ACP primers and does not utilize acetyl-CoA as a primer. No substrates: acetyl-CoA, butyryl-CoA, or isovaleryl-CoA
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-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(1-bromoheptyl)-4-(4-[[(2,4-difluorophenyl)methyl]amino]phenyl)-1H-pyrrole-2-carboxylic acid
compound exhibits strong inhibition on the growth of Mycobacterium tuberculosis H37Rv at 2 and at 4 weeks
1-(1-bromohexyl)-4-(4-[[(3,5-difluorophenyl)methyl]amino]phenyl)-1H-pyrrole-2-carboxylic acid
compound exhibits strong inhibition on the growth of Mycobacterium tuberculosis H37Rv at 2 and at 4 weeks
1-(1-bromooctyl)-4-(4-[[(2,5-difluorophenyl)methyl]amino]phenyl)-1H-pyrrole-2-carboxylic acid
compound exhibits strong inhibition on the growth of Mycobacterium tuberculosis H37Rv at 2 and at 4 weeks
1-(3-carboxypropyl)-4-[4-[(3,5-difluorophenyl)methoxy]phenyl]-1H-pyrrole-2-carboxylic acid
compound possesses good in vitro antimycobacterial activity, MIC value 12.5 microg/ml
1-[(3-chlorophenyl)methyl]-4-(4-[[(2,4-difluorophenyl)methyl]amino]phenyl)-1H-pyrrole-2-carboxylic acid
compound exhibits strong inhibition on the growth of Mycobacterium tuberculosis H37Rv at 2 and at 4 weeks
1-[(4-chlorophenyl)methyl]-4-(4-[[(2,4-difluorophenyl)methyl]amino]phenyl)-1H-pyrrole-2-carboxylic acid
compound exhibits strong inhibition on the growth of Mycobacterium tuberculosis H37Rv at 2 and at 4 weeks
[4-(1,4-dihydroxynaphthalene-2-sulfonyl)phenyl]carbamic acid
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additional information
2-tosylnaphthalene-1,4-diol analogues are reversible inhibitors (30 nM-5 microM) of the Mycobacterium tuberculosis and Plasmodium falciparum FabH enzymes. 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 Escherichia coli FabH, EC 2.3.1.180
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0038
1-([[(2-hydroxyethyl)disulfanyl]carbonyl]oxy)octane
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0027
11-[[(decyldisulfanyl)carbonyl]oxy]undecanoic acid
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0024
11-[[(decyloxy)carbonyl]disulfanyl]undecanoic acid
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000036
2-(4-chlorobenzene-1-sulfonyl)naphthalene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000085
2-(4-methylbenzene-1-sulfonyl)anthracene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.00000061
2-(4-methylbenzene-1-sulfonyl)naphthalene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000002
2-(4-methylbenzene-1-sulfonyl)naphthalene-1,4-dione
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000031
2-(4-propylbenzene-1-sulfonyl)naphthalene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000028
2-(benzenesulfonyl)naphthalene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000035
2-(methanesulfonyl)naphthalene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000015
2-(naphthalene-2-sulfonyl)naphthalene-1,4-diol
Mycobacterium tuberculosis
pH 7.4, 23°C
0.0000035
3-(1,4-dihydroxynaphthalene-2-sulfonyl)propanoic acid
Mycobacterium tuberculosis
pH 7.4, 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00006
substrates arachoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.0004
substrates hexanoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.0006
substrates stearoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.0013
0.00174
substrates hexanoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.0022
substrates tetradecanoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.00549
substrates octanoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.006
substrates octanoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.00616
substrates decanoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.0063
substrates decanoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.00724
substrates dodecanoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.008
substrates dodecanoyl-CoA and malonyl-[ACP], pH 7, 37°C
0.009
substrates arachoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.00927
substrates palmitoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.00946
substrates tetradecanoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.0104
substrates stearoyl-CoA and malonyl-[AcpM], pH 7, 37°C
0.0013
substrates palmitoyl-CoA and malonyl-[ACP], pH 7, 37°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
brenda
-
Uniprot
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
ordering or closing of the FabH on the substrate or inhibitor is required for efficient reaction with the active site cysteine. The acyl-CoA reactant, in principle, could synchronously bind to both arms of the exposed substrate binding site. Movement to the closed form, and reaction with Cys112, would follow. CoA product released from the mouth of the pantetheinate channel would then complete the first stage of the reaction
metabolism
reaction occurs at both subunits and shows strict specificity for dodecyl-CoA
metabolism
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reaction occurs at both subunits and shows strict specificity for dodecyl-CoA
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metabolism
-
ordering or closing of the FabH on the substrate or inhibitor is required for efficient reaction with the active site cysteine. The acyl-CoA reactant, in principle, could synchronously bind to both arms of the exposed substrate binding site. Movement to the closed form, and reaction with Cys112, would follow. CoA product released from the mouth of the pantetheinate channel would then complete the first stage of the reaction
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FABH_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
335
0
34873
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
2 * 36903, ESI mass spectrometry and crystallization data
dimer
-
2 * 36903, ESI mass spectrometry and crystallization data
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
FabH is efficiently phosphorylated in vitro by several mycobacterial Ser/Thr protein kinases, particularly by PknF and PknA, as well as in vivo. Residues Thr45 is the unique phosphoacceptor. Thr 45 is located at the entrance of the substrate channel
phosphoprotein
-
FabH is efficiently phosphorylated in vitro by several mycobacterial Ser/Thr protein kinases, particularly by PknF and PknA, as well as in vivo. Residues Thr45 is the unique phosphoacceptor. Thr 45 is located at the entrance of the substrate channel
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of mutant C112A with lauroyl-coenzyme A. An elongated channelextending from the mutated active-site cysteine defines the acyl group binding locus. CoA lies in a second channel, bound primarily through interactions of its nucleotide group at the enzyme surface
strucure of FabH with CoAdecyl disulfide inhibitor. The decyl chain binds in acyl-binding channels of both subunits through disulfide linkage to the active site cysteine. Both subunits of FabH can react with substrates or inhibitor
strucure to 2.1 A resolution. A CoA/malonyl-ACP-binding channel leads from the enzyme surface to the buried active-site cysteine residue, and a second hydrophobic channel leads from the active site. In the ecFabH structure, this channel is blocked by a phenylalanine residue, whereas in Microbacterium tuberculosisFabH, this residue is a threonine, which permits binding of longer acyl chains
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A246F
mutation introduces a large obstructive group into the pantetheinate channel, no detectable catalytic activity
C112A
C122A
A246F
-
mutation introduces a large obstructive group into the pantetheinate channel, no detectable catalytic activity
-
C112A
C122A
C112A
mutation of active site residue, no detectable activity
C112A
-
mutation of active site residue, no detectable activity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
discontinuous assay for the FabH enzyme that eliminates the need for the washing steps or specialty scintillation proximity assay beads and the preparation of acyl carrier proteins. The 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
analysis
-
discontinuous assay for the FabH enzyme that eliminates the need for the washing steps or specialty scintillation proximity assay beads and the preparation of acyl carrier proteins. The 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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sachdeva, S.; Musayev, F.; Alhamadsheh, M.; Neel Scarsdale, J.; Tonie Wright, H.; Reynolds, K.
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 (P9WNG3), Mycobacterium tuberculosis ATCC 25618 (P9WNG3)
brenda
Alhamadsheh, M.; Waters, N.; Sachdeva, S.; Lee, P.; Reynolds, K.
Synthesis and biological evaluation of novel sulfonyl-naphthalene-1,4-diols as FabH inhibitors
Bioorg. Med. Chem. Lett.
18
6402-6405
2008
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Alhamadsheh, M.; Musayev, F.; Komissarov, A.; Sachdeva, S.; Wright, H.; Scarsdale, N.; Florova, G.; Reynolds, K.
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes
Chem. Biol.
14
513-524
2007
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Sachdeva, S.; Musayev, F.; Alhamadsheh, M.; Scarsdale, J.; Wright, H.; Reynolds, K.
Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH
Chem. Biol.
15
402-412
2008
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis ATCC 25618 (P9WNG3)
brenda
Zhang, X.; Yu, H.; Zhong, W.; Wang, L.; Li, S.
Structure-based design, synthesis of novel inhibitors of Mycobacterium tuberculosis FabH as potential anti-tuberculosis agents
Chin. Chem. Lett.
20
1019-1022
2009
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis ATCC 25618 (P9WNG3)
-
brenda
Choi, K.; Kremer, L.; Besra, G.; Rock, C.
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 (P9WNG3), Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Scarsdale, J.; Kazanina, G.; He, X.; Reynolds, K.; Wright, H.
Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III
J. Biol. Chem.
276
20516-20522
2001
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Brown, A.; Sridharan, S.; Kremer, L.; Lindenberg, S.; Dover, L.; Sacchettini, J.; Besra, G.
Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH Factors influencing catalysis and substrate specificity
J. Biol. Chem.
280
32539-32547
2005
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis H37Rv (P9WNG3)
brenda
Veyron-Churlet, R.; Molle, V.; Taylor, R.; Brown, A.; Besra, G.; 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 H37Rv (P9WNG3)
brenda
Musayev, F.; Sachdeva, S.; Scarsdale, J.; Reynolds, K.; Wright, H.
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 ATCC 25618 (P9WNG3)
brenda
Sachdeva, S.; Reynolds, K.
Mycobacterium tuberculosis beta-ketoacyl acyl carrier protein synthase III (mtFabH) assay principles and method
Methods Mol. Med.
142
205-213
2008
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis ATCC 25618 (P9WNG3)
brenda
Liu, Y.; Zhong, W.; Li, R.; Li, S.
Synthesis of potent inhibitors of beta-ketoacyl-acyl carrier protein synthase III as potential antimicrobial agents
Molecules
17
4770-4781
2012
Mycobacterium tuberculosis (P9WNG3), Mycobacterium tuberculosis ATCC 25618 (P9WNG3)
brenda
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