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EC Tree
IUBMB Comments The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasA differs from KasB [EC 2.3.1.294, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II], by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
The expected taxonomic range for this enzyme is: Mycobacteriaceae
Reaction Schemes
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein]
+
=
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein]
+
+
Synonyms
beta-ketoacyl-acyl carrier protein synthase, beta-ketoacyl acp synthase, rv2245,
more
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beta-ketoacyl ACP synthase
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beta-ketoacyl ACP synthase I
beta-ketoacyl acyl carrier protein synthase
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beta-ketoacyl-ACP synthase
beta-ketoacyl-AcpM synthase
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beta-ketoacyl-AcpM synthase A
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beta-ketoacyl-acyl carrier protein synthase
beta-ketoacyl-acyl carrier protein synthase KasA
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beta-ketoacyl-acyl-carrier protein synthase
beta-ketoacylacyl synthase
beta-ketoacyl ACP synthase I
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beta-ketoacyl ACP synthase I
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beta-ketoacyl-ACP synthase
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beta-ketoacyl-ACP synthase
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beta-ketoacyl-acyl carrier protein synthase
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beta-ketoacyl-acyl carrier protein synthase
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beta-ketoacyl-acyl carrier protein synthase
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beta-ketoacyl-acyl carrier protein synthase
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beta-ketoacyl-acyl-carrier protein synthase
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beta-ketoacyl-acyl-carrier protein synthase
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beta-ketoacylacyl synthase
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beta-ketoacylacyl synthase
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KasA
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Rv2245
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an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + a holo-[acyl-carrier protein]
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ultra-long-chain mono-unsaturated fattyl acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
The enzyme is part of the fatty acid synthase (FAS) II system of mycobacteria, which extends modified products of the FAS I system, eventually forming meromycolic acids that are incorporated into mycolic acids. Meromycolic acids consist of a long chain, typically 50-60 carbons, which is functionalized by different groups.Two 3-oxoacyl-(acyl carrier protein) synthases function within the FAS II system, encoded by the kasA and kasB genes. The two enzymes share some sequence identity but function independently on separate sets of substrates. KasA differs from KasB [EC 2.3.1.294, meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II], by preferring shorter (C-22 to C-36) and more saturated (only one double bond) substrates.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + palmitoyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
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?
C12:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
C20:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
C4:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
myristoyl-[acyl-carrier protein] + biotinylated malonyl-[acyl-carrier protein]
?
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?
palmitoyl-CoA + malonyl-[acyl-carrier protein AcpM]
?
palmitoyl-CoA + malonyl-[acyl-carrier protein from Escherichia coli]
?
palmitoyl-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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?
additional information
?
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an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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-
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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-
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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C16-C26
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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-
-
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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C16-C26
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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?
C12:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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?
C12:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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?
C20:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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best substrate
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?
C20:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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best substrate
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?
C4:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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very low activity
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?
C4:0-[acyl-carrier protein from Escherichia coli] + malonyl-[acyl-carrier protein from Escherichia coli]
?
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very low activity
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?
palmitoyl-CoA + malonyl-[acyl-carrier protein AcpM]
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?
palmitoyl-CoA + malonyl-[acyl-carrier protein AcpM]
?
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?
palmitoyl-CoA + malonyl-[acyl-carrier protein from Escherichia coli]
?
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weak activity
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?
palmitoyl-CoA + malonyl-[acyl-carrier protein from Escherichia coli]
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weak activity
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?
additional information
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the enzyme catalyzes the condensation steps from C18 to C34 long-chain fatty acids
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?
additional information
?
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the enzyme catalyzes the condensation steps from C18 to C34 long-chain fatty acids
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
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-
-
-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + palmitoyl-[acyl-carrier protein AcpM]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein AcpM]
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?
additional information
?
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an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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-
-
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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-
-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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C16-C26
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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-
-
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?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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C16-C26
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-
?
an ultra-long-chain mono-unsaturated acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
an ultra-long-chain mono-unsaturated 3-oxo-fatty acyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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?
additional information
?
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the enzyme catalyzes the condensation steps from C18 to C34 long-chain fatty acids
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-
?
additional information
?
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the enzyme catalyzes the condensation steps from C18 to C34 long-chain fatty acids
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NADPH
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0.05 mM NADPH is used in assay conditions
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(5R)-3-acetyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-butanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-ethyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-hexadecanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-[2-(4-chlorophenyl)ethyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-[4-(4-chlorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-[4-(4-fluorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-[4-([1,1'-biphenyl]-4-yl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-3-[6-([1,1'-biphenyl]-4-yl)hexanoyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(propan-2-yl)thiophen-2(5H)-one
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(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(trifluoroacetyl)thiophen-2(5H)-one
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(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-[2-(4-methylphenyl)ethyl]thiophen-2(5H)-one
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(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
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2-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carbonyl]benzoic acid
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4-[(4-fluorobenzene-1-sulfonyl)amino]-N-[[1-(4-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophen-3-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]benzamide
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methyl (5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carboxylate
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platensimycin
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natural product inhibitor
cerulenin
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natural product inhibitor
cerulenin
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41-44% inhibition at 0.1 mM
thiolactomycin
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natural product inhibitor, binding analysis with wild-type and mutant enzymes, overview. Structure-activity relationships of thiolactomycin and derivatives
thiolactomycin
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90-98% inhibition at 0.1 mM
thiolactomycin
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slow onset inhibitor
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DMSO
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about 130% activity at 2.5% (v/v) DMSO
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Tuberculosis
Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid.
Tuberculosis
Modeling the Interactions of Herbal Drugs to beta-ketoacyl ACP Synthase of Mycobacterium tuberculosis H37Rv.
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0.005
biotinylated malonyl-[acyl-carrier protein]
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at pH 6.8 and 37°C
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0.0025
C20:0-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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0.0135
malonyl-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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0.003
myristoyl-[acyl-carrier protein]
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at pH 6.8 and 37°C
0.0026
palmitoyl-[acyl-carrier protein AcpM]
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at pH 8.5 and 25°C
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0.0032
palmitoyl-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
-
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0.075
C20:0-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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0.08
malonyl-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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0.533
palmitoyl-[acyl-carrier protein AcpM]
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at pH 8.5 and 25°C
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0.088
palmitoyl-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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30
C20:0-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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5.83
malonyl-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
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205
palmitoyl-[acyl-carrier protein AcpM]
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at pH 8.5 and 25°C
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28.33
palmitoyl-[acyl-carrier protein from Escherichia coli]
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at pH 6.8 and 37°C
-
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0.0082
(5R)-3-acetyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0652
(5R)-3-butanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.357
(5R)-3-ethyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.105
(5R)-3-hexadecanoyl-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.4
(5R)-3-[2-(4-chlorophenyl)ethyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0774
(5R)-3-[4-(4-chlorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.069
(5R)-3-[4-(4-fluorophenyl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0138
(5R)-3-[4-([1,1'-biphenyl]-4-yl)butyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.008
(5R)-3-[6-([1,1'-biphenyl]-4-yl)hexanoyl]-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.305
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(propan-2-yl)thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0121
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-(trifluoroacetyl)thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.0928
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-3-[2-(4-methylphenyl)ethyl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.047
(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]thiophen-2(5H)-one
-
pH and temperature not specified in the publication
0.102
2-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carbonyl]benzoic acid
-
pH and temperature not specified in the publication
0.032
4-[(4-fluorobenzene-1-sulfonyl)amino]-N-[[1-(4-[(5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophen-3-yl]butyl)-1H-1,2,3-triazol-4-yl]methyl]benzamide
-
pH and temperature not specified in the publication
0.0219
methyl (5R)-4-hydroxy-5-methyl-5-[(1E)-2-methylbuta-1,3-dien-1-yl]-2-oxo-2,5-dihydrothiophene-3-carboxylate
-
pH and temperature not specified in the publication
0.1754
thiolactomycin
-
pH and temperature not specified in the publication
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0.0047 - 0.252
thiolactomycin
0.0047
thiolactomycin
Mycobacterium tuberculosis
-
at pH 6.8 and 37°C
0.02
thiolactomycin
Mycobacterium tuberculosis
-
at pH 6.8 and 37°C
0.252
thiolactomycin
Mycobacterium tuberculosis
-
apoenzyme, at pH 8.5 and 25°C
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0.0057
-
with palmitoyl-CoA as substrate, at pH 6.8 and 37°C
0.0878
-
palmitoyl-[acyl-carrier protein] as substrate, at pH 6.8 and 37°C
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 42
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the enzyme displays about 2-3fold higher specific activities at 37°C compared with 30 or 42°C
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brenda
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brenda
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brenda
cf. EC 2.3.1.41
SwissProt
brenda
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brenda
cf. EC 2.3.1.41
SwissProt
brenda
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-
-
brenda
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-
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brenda
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malfunction
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depletion of the enzyme leads to mycobacterial cell lysis and inhibition of alpha and epoxy mycolate biosynthesis and to accumulation of alpha'-mycolates
malfunction
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depletion of the enzyme leads to mycobacterial cell lysis and inhibition of alpha and epoxy mycolate biosynthesis and to accumulation of alpha'-mycolates
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metabolism
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an essential enzyme in the mycobacterial fatty acid biosynthesis (FAS-II) pathway, type II fatty acid biosynthesis pathway overview
metabolism
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key enzyme of mycolic acid biosynthesis
metabolism
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the enzyme is involved in fatty acid and mycolic acid biosynthesis
metabolism
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when KasB is coexpressed with enzyme KasA, it appears to be capable of facilitating the production of lipids of the length of full meromycolic acids. KasB therefore may accept primers directly from KasA that average 40 carbons in length. KasA and KasB thus function in tandem to carrier out acyl chain elongation to achieve meromycolic acid synthesis from acyl primers provided by type I fatty acid synthase system
metabolism
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the enzyme is involved in fatty acid and mycolic acid biosynthesis
-
metabolism
-
when KasB is coexpressed with enzyme KasA, it appears to be capable of facilitating the production of lipids of the length of full meromycolic acids. KasB therefore may accept primers directly from KasA that average 40 carbons in length. KasA and KasB thus function in tandem to carrier out acyl chain elongation to achieve meromycolic acid synthesis from acyl primers provided by type I fatty acid synthase system
-
metabolism
-
key enzyme of mycolic acid biosynthesis
-
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KASA_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
416
0
43316
Swiss-Prot
-
KASA_MYCLE
Mycobacterium leprae (strain TN)
416
0
43470
Swiss-Prot
-
KASA_MYCTE
Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
416
0
43316
Swiss-Prot
-
KASA_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
416
0
43316
Swiss-Prot
-
KASA_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
416
0
43316
Swiss-Prot
-
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?
-
x * 43000, SDS-PAGE
?
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x * 43300, calculated from amino acid sequence
?
-
x * 43000, SDS-PAGE
-
?
-
x * 45000, SDS-PAGE
-
?
-
x * 43300, calculated from amino acid sequence
-
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apo-enzyme and mutant C171Q bound to thiolactomycin, vapor diffusion method, using 10% (v/v) isopropanol, 0.2 M NaCl, 0.1 M HEPES pH 7.5 and 10 mM tris(2-carboxyethyl)phosphine hydrochloride (for apoenzyme), or 20% (w/v) polyethylene glycol 3350 and 0.2 M potassium formate (for mutant C171Q)
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C171Q
-
acyl-enzyme mimic
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D66N
-
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
-
G269S
-
the S mutation may affect targeting of the inhibitor thiolactomycin to the enzyme
-
C171Q
-
site-directed mutagenesis, ligand binding and active site structure analysis
C171Q
-
the mutant mimics the acyl-enzyme intermediate
D66N
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
D66N
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
F413L
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
F413L
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
G269S
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
G269S
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
G269S
-
the S mutation may affect targeting of the inhibitor thiolactomycin to the enzyme
G312S
dimer non-active site mutant protein displays much more structural flexibility than wild type at the ligand binding site
G312S
-
the mutation occurs in isonicotinic acid hydrazide-resistant clinical isolates of Mycobacterium tuberculosis
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HisTrap column chromatography, MonoQ column chromatography and Superdex S200 gel filtration
metal ion affinity chromatography and G-25 resin gel filtration
-
Q-Sepharose column chromatography and HiTrap column chromatography
-
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expressed in Escherichia coli BL21(DE3) cells
-
expressed in Mycobacterium bovis BCG vaccine strain 1173P2
-
expressed in Mycobacterium smegmatis
-
expressed in Mycobacterium smegmatis strain mc2155
gene kasA, recombinant expression in Mycobacterium smegmatis strain mc2155
-
expressed in Mycobacterium smegmatis strain mc2155
-
expressed in Mycobacterium smegmatis strain mc2155
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Kapilashrami, K.; Bommineni, G.R.; Machutta, C.A.; Kim, P.; Lai, C.T.; Simmerling, C.; Picart, F.; Tonge, P.J.
Thiolactomycin-based beta-ketoacyl-AcpM synthase A (KasA) inhibitors: fragment-based inhibitor discovery using transient one-dimensional nuclear overhauser effect NMR spectroscopy
J. Biol. Chem.
288
6045-6052
2013
Mycobacterium tuberculosis
brenda
Jayaraman, M.; Rajendra, S.; Ramadas, K.
Structural insight into conformational dynamics of non-active site mutations in KasA A Mycobacterium tuberculosis target protein
Gene
720
144082
2019
Mycobacterium tuberculosis (P9WQD9), Mycobacterium tuberculosis H37Rv (P9WQD9)
brenda
Bhatt, A.; Kremer, L.; Dai, A.Z.; Sacchettini, J.C.; Jacobs, W.R.
Conditional depletion of KasA, a key enzyme of mycolic acid biosynthesis, leads to mycobacterial cell lysis
J. Bacteriol.
187
7596-7606
2005
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2155
brenda
Kremer, L.; Douglas, J.D.; Baulard, A.R.; Morehouse, C.; Guy, M.R.; Alland, D.; Dover, L.G.; Lakey, J.H.; Jacobs, W.R.; Brennan, P.J.; Minnikin, D.E.; Besra, G.S.
Thiolactomycin and related analogues as novel anti-mycobacterial agents targeting KasA and KasB condensing enzymes in Mycobacterium tuberculosis
J. Biol. Chem.
275
16857-16864
2000
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Schaeffer, M.L.; Agnihotri, G.; Volker, C.; Kallender, H.; Brennan, P.J.; Lonsdale, J.T.
Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB
J. Biol. Chem.
276
47029-47037
2001
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Machutta, C.A.; Bommineni, G.R.; Luckner, S.R.; Kapilashrami, K.; Ruzsicska, B.; Simmerling, C.; Kisker, C.; Tonge, P.J.
Slow onset inhibition of bacterial beta-ketoacyl-acyl carrier protein synthases by thiolactomycin
J. Biol. Chem.
285
6161-6169
2010
Mycobacterium tuberculosis
brenda
Mdluli, K.; Slayden, R.A.; Zhu, Y.; Ramaswamy, S.; Pan, X.; Mead, D.; Crane, D.D.; Musser, J.M.; Barry, C.E.
Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid
Science
280
1607-1610
1998
Mycobacterium tuberculosis
brenda
Luckner, S.; Machutta, C.; Tonge, P.; Kisker, C.
Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin
Structure
17
1004-1013
2009
Mycobacterium tuberculosis (P9WQD9), Mycobacterium tuberculosis H37Rv (P9WQD9)
brenda
Slayden, R.; Barry III, C.
The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis
Tuberculosis
82
149-160
2002
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Schaeffer, M.L.; Carson, J.D.; Kallender, H.; Lonsdale, J.T.
Development of a scintillation proximity assay for the Mycobacterium tuberculosis KasA and KasB enzymes involved in mycolic acid biosynthesis
Tuberculosis
84
353-360
2004
Mycobacterium tuberculosis
brenda
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