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3-ketoacyl acyl synthase II
3-ketoacyl-ACP synthase
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3-ketoacyl-ACP synthase 2
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3-ketoacyl-ACP synthase II
3-oxoacyl-(acylcarrier protein) synthase II
3-oxoacyl-ACP synthase II
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B-ketoacyl-ACP synthase II
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beta-ketoacyl ACP-synthase II
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beta-ketoacyl acyl carrier protein synthase II
beta-ketoacyl acyl-carrier protein synthase II
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beta-ketoacyl synthase II
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beta-ketoacyl-(acyl-carrier-protein) synthase II
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beta-ketoacyl-ACP synthase FabF3
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KAS-II homologue
beta-ketoacyl-ACP synthase II
beta-ketoacyl-acyl carrier protein synthase I/II
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beta-ketoacyl-acyl carrier protein synthase II
beta-ketoacyl-acyl carrier protein synthases II
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beta-ketoacyl-acyl carrier protein synthetase II
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beta-ketoacyl-acyl-carrier protein synthase II
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beta-ketoacyl-acyl-carrier-protein synthase II
beta-ketoacyl-[ACP] synthase II
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beta-ketoacyl-[ACP] synthase-II
beta-ketoacyl-[acyl carrier protein (ACP)] synthase II
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beta-ketoacyl-[acyl-carrier protein (ACP)] synthase II
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beta-ketoacyl-[acyl-carrier-protein] synthase II
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FabF elongation condensing enzyme
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FabF of type II fatty acid biosynthesis
fatty acid synthesis type II
3-ketoacyl acyl synthase II
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3-ketoacyl acyl synthase II
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3-ketoacyl acyl synthase II
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3-ketoacyl-ACP synthase II
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3-ketoacyl-ACP synthase II
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3-oxoacyl-(acylcarrier protein) synthase II
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3-oxoacyl-(acylcarrier protein) synthase II
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beta-ketoacyl acyl carrier protein synthase II
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beta-ketoacyl acyl carrier protein synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-ACP synthase II
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beta-ketoacyl-acyl carrier protein synthase II
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beta-ketoacyl-acyl carrier protein synthase II
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beta-ketoacyl-acyl carrier protein synthase II
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beta-ketoacyl-acyl carrier protein synthase II
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beta-ketoacyl-acyl carrier protein synthase II
Q7CJ22
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beta-ketoacyl-acyl-carrier-protein synthase II
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beta-ketoacyl-acyl-carrier-protein synthase II
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beta-ketoacyl-acyl-carrier-protein synthase II
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beta-ketoacyl-acyl-carrier-protein synthase II
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beta-ketoacyl-acyl-carrier-protein synthase II
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beta-ketoacyl-[ACP] synthase-II
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beta-ketoacyl-[ACP] synthase-II
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FabB
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FabF
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FabF of type II fatty acid biosynthesis
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FabF of type II fatty acid biosynthesis
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FabF of type II fatty acid biosynthesis
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FabF1
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FASII
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fatty acid synthesis type II
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fatty acid synthesis type II
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fatty acid synthesis type II
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KAS II
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KAS-II
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KASII
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
elongation condensing enzyme, catalytic mechanism involving Cys134, His337, and His303, forming the catalytic triad, as well as Phe396, and a water molecule bound to the active site, analysis of residues involved in the different reaction steps, overview
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
two-stage mechanism, driven by a dipole moment, the active site cysteine, Cys164 in YpFabF 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, His304 and His341, are thought to stabilise the fatty acyl intermediate during transition states
Q7CJ22
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(Z)-hexadec-9-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
(Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacetyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
Substrates: -
Products: -
?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
Substrates: -
Products: -
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decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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Substrates: -
Products: -
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dodec-5-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
Substrates: -
Products: -
?
malonyl-ACP + lauroyl-ACP
?
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Substrates: -
Products: -
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malonyl-CoA + lauroyl-CoA
?
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Substrates: -
Products: -
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malonyl-CoA + palmitoyl-[acyl-carrier protein]
?
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Substrates: -
Products: -
?
malonyl-phosphopantetheine + lauroyl-CoA
?
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Substrates: -
Products: -
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malonyl-phosphopantetheine-14-mer + lauroyl-CoA
?
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Substrates: -
Products: -
?
malonyl-phosphopantetheine-16-mer + lauroyl-CoA
?
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Substrates: -
Products: -
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malonyl-phosphopantetheine-8-mer + lauroyl-CoA
?
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Substrates: -
Products: -
?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
palmitoleoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-vaccenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
Substrates: -
Products: -
?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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Substrates: -
Products: -
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tetradec-7-enoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
Substrates: -
Products: -
?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
Substrates: -
Products: -
?
additional information
?
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
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Substrates: -
Products: -
?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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Substrates: -
Products: -
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myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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Substrates: -
Products: -
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additional information
?
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Substrates: KASII elongates 16:0-acyl carrier protein to 18:0-acyl carrier protein in the plastid, where it competes with three other enzymes at the first major branch point in fatty acid biosynthesis
Products: -
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additional information
?
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Substrates: KAS II catalyzes the elongation of 16:0 fatty acid-[acyl-carrier-protein] to 18:0 fatty acid-[acyl-carrier-protein] in plastids
Products: -
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additional information
?
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Substrates: KAS II catalyzes the elongation of 16:0 fatty acid-[acyl-carrier-protein] to 18:0 fatty acid-[acyl-carrier-protein] in plastids
Products: -
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additional information
?
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Substrates: the enzyme is involved in elongation of palmitoyl-[acyl-carrier-protein] to stearoyl-[acyl-carrier-protein]
Products: -
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additional information
?
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Substrates: FabF1 is able to catalyze all of the elongation reactions required in the synthesis of saturated fatty acids. The single 3-ketoacyl-[acyl-carrier-protein] synthase FabF of this bacterium performs the elongation functions required in both branches of the fatty acid synthetic pathway. The enzyme can both elongate palmitoleoyl-[acyl-carrier-protein] to cis-vaccenoyl-[acyl-carrier-protein] and elongate the cis double bond containing the product of FabA
Products: -
?
additional information
?
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Substrates: of the enzymes encoded by fabF homologues designated as CAC3573, CAC2008 and CAA0093, only the first of these genes, fabF1, functions in fatty acid synthesis and can functionally replace Escherichia coli FabF in vivo, overview
Products: -
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additional information
?
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Substrates: altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. F-ACP is a modification of ACP that is detected when beta-ketoacyl-ACP synthase II activity is impaired
Products: -
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additional information
?
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Substrates: beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
Products: -
?
additional information
?
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Substrates: beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
Products: -
?
additional information
?
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Substrates: proposed role of the enzyme in the modulation of fatty acid synthesis by temperature
Products: -
?
additional information
?
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Substrates: the enzyme carries out the elongation step in fatty acid synthesis
Products: -
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additional information
?
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Substrates: the enzyme carries out the elongation step in fatty acid synthesis
Products: -
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additional information
?
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Substrates: PfFabB/F does not elongate C16DELTA9-[acyl-carrier-protein], substrate specificity, overview
Products: -
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additional information
?
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Substrates: enzyme forms FabF1 and FabB are functionally overlapping but not identical. FabF1 is largely a functional replacement for FabB but differs from the latter in that it does not have a severe detrimental impact on physiology
Products: -
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additional information
?
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Substrates: enzyme forms FabF1 and FabB are functionally overlapping but not identical. FabF1 is largely a functional replacement for FabB but differs from the latter in that it does not have a severe detrimental impact on physiology
Products: -
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additional information
?
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Substrates: the enzyme plays a key role in synthesis of C18 fatty acids
Products: -
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additional information
?
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Substrates: enzyme is inactive with stearoyl-[acyl-carrier-protein]
Products: -
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additional information
?
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Substrates: FabF produces C14 long-chain beta-ketoacyl-ACP
Products: -
?
additional information
?
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Substrates: analysis of interaction between FabF and the acyl-carrier protein
Products: -
?
additional information
?
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Q7CJ22
Substrates: enzyme substrate specificity, overview
Products: -
?
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
? + CO2 + [acyl-carrier protein]
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Substrates: -
Products: -
?
additional information
?
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a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
Substrates: -
Products: -
?
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a (Z)-3-oxooctadeca-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: KASII elongates 16:0-acyl carrier protein to 18:0-acyl carrier protein in the plastid, where it competes with three other enzymes at the first major branch point in fatty acid biosynthesis
Products: -
?
additional information
?
-
Substrates: KAS II catalyzes the elongation of 16:0 fatty acid-[acyl-carrier-protein] to 18:0 fatty acid-[acyl-carrier-protein] in plastids
Products: -
?
additional information
?
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Substrates: KAS II catalyzes the elongation of 16:0 fatty acid-[acyl-carrier-protein] to 18:0 fatty acid-[acyl-carrier-protein] in plastids
Products: -
?
additional information
?
-
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Substrates: the enzyme is involved in elongation of palmitoyl-[acyl-carrier-protein] to stearoyl-[acyl-carrier-protein]
Products: -
?
additional information
?
-
-
Substrates: FabF1 is able to catalyze all of the elongation reactions required in the synthesis of saturated fatty acids. The single 3-ketoacyl-[acyl-carrier-protein] synthase FabF of this bacterium performs the elongation functions required in both branches of the fatty acid synthetic pathway. The enzyme can both elongate palmitoleoyl-[acyl-carrier-protein] to cis-vaccenoyl-[acyl-carrier-protein] and elongate the cis double bond containing the product of FabA
Products: -
?
additional information
?
-
-
Substrates: altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. F-ACP is a modification of ACP that is detected when beta-ketoacyl-ACP synthase II activity is impaired
Products: -
?
additional information
?
-
Substrates: beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
Products: -
?
additional information
?
-
-
Substrates: beta-ketoacyl-acyl carrier protein synthase II is centrally involved in the temperature regulation of the fatty acid composition of the membrane phospholipid of Escherichia coli. The genetic locus of the Cvc lesion is designated fabF
Products: -
?
additional information
?
-
Substrates: proposed role of the enzyme in the modulation of fatty acid synthesis by temperature
Products: -
?
additional information
?
-
Substrates: the enzyme carries out the elongation step in fatty acid synthesis
Products: -
?
additional information
?
-
-
Substrates: the enzyme carries out the elongation step in fatty acid synthesis
Products: -
?
additional information
?
-
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Substrates: the enzyme plays a key role in synthesis of C18 fatty acids
Products: -
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2E)-3-(3-chlorophenyl)-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]prop-2-enamide
ME0619
1,3-dichloro-7-(2,4-dihydroxy-6-methylphenyl)-2,4,6,9-tetrahydroxy-12,12-dimethyltetracen-5(12H)-one
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i.e. fasamycin B
1-chloro-7-(2,4-dihydroxy-6-methylphenyl)-2,4,6,9-tetrahydroxy-12,12-dimethyltetracen-5(12H)-one
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i.e. fasamycin A
2-[(2R)-4-ethyl-3-hydroxy-2-[(1E)-2-methylbuta-1,3-dien-1-yl]-5-oxo-2,5-dihydrothiophen-2-yl]acetamide
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3,6-dichloro-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]-1-benzothiophene-2-carboxamide
ME0640
3,6-dichloro-N-[5-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]pyridin-2-yl]-1-benzothiophene-2-carboxamide
ME0518
3-(benzoylamino)-2-hydroxybenzoic acid
binds outside the active site of the enzyme, binding structure with wild-type and C164Q mutant enzymes, overview. Access to the depths of the active site of the PaFabF apoenzyme is restricted by the conformations of Phe230 and Phe400. 3-(benzoylamino)-2-hydroxybenzoic acid/Mg2+ ion pair selectively binds into and perhaps contributes to the formation of a stable binding site on the surface of the enzyme distant from the active site, from which it is likely to be occluded by steric hindrance
3-benzamido-2-hydroxybenzoic acid
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5-chloro-2-(2,4-dichlorophenoxy)phenol
Acyl carrier protein
0.0017 mM, 50% inhibition of myristic acid transfer from myristoyl-[acyl-carrier protein] to wild-type enzyme
arsenite
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1 mM, 42% inhibition
casticin
i.e. 5-hydroxy-2-(3-hydroxy-4-methoxyphenyl)-3,6,7-trimethoxy-4H-chromen-4-one
dihydroplatensimycin
IC50: 97 nM
iodoacetamide
prior incubation of the enzymes with fatty acyl thioesters prevents inhibition
NEM
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5 mM, complete inhibition
PCMB
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1 mM, complete inhibition
5-chloro-2-(2,4-dichlorophenoxy)phenol
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Triclosan
5-chloro-2-(2,4-dichlorophenoxy)phenol
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Triclosan
cerulenin
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0.1 mM, 50% inhibition
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
binding structure with mutant C163Q
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
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0.05 mM, 50% inhibition
cerulenin
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originally isolated from the fungus Cephalosporium caerulensand, an irreversible inhibitor of FabF
cerulenin
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blocking active site cysteine
fasamycin A
-
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fasamycin B
-
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phomallenic acid C
-
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platencin
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exhibits a broad-spectrum Gram-positive antibacterial activity through inhibition of fatty acid biosynthesis, targets the two essential proteins, beta-ketoacyl-[acyl carrier protein] synthase II and III, i.e. FabF and FabH, FabF IC50: 113 nM, overview
platencin A1
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also active against FabH, EC 2.3.1.180
platencin A1
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also active against FabH, EC 2.3.1.180
platencin A1
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also active against FabH, EC 2.3.1.180
platensimycin
-
platensimycin
from Streptomyces platensis, IC50: 160 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with the acyl-enzyme intermediate of the target protein, a specific conformational change that occurs on acylation must take place before the inhibitor can bind, overview, platensimycin shows no cross-resistance to other key antibiotic-resistant strains, binding structure with mutant C163Q
platensimycin
a natural product inhibitor
platensimycin
-
from Streptomyces platensis, IC50: 48 nM, anti-bacterial effect is exerted through the selective targeting of beta-ketoacyl-[acyl-carrier-protein] synthase I/II, FabF/B, in the synthetic pathway of fatty acids, platensimycin interacts specifically with the acyl-enzyme intermediate of the target protein, a specific conformational change that occurs on acylation must take place before the inhibitor can bind, overview, platensimycin shows no cross-resistance to other key antibiotic-resistant strains
platensimycin
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from a strain of Streptomyces platensis MA7339, specifically targets FabF, IC50: 290 nM, exhibits Gram-positive antibacterial activity
thiolactomycin
-
-
thiolactomycin
binding structure with mutant C163Q, IC50: 1.1 mM
T3010
-
-
additional information
not inhibited by triclosan
-
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
-
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
-
in vivo inhibition assays
-
additional information
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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
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additional information
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not inhibited by platensimycin
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additional information
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not inhibited by platensimycin
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additional information
Q7CJ22
inhibitor interaction with the active site, structure analysis, docking study, overview
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0.014
acetyl-[acyl-carrier protein]
pH 7.2
0.017
cis-3-decenoyl-[acyl-carrier protein]
pH 7.2
0.0133
decanoyl-[acyl-carrier protein]
-
-
0.024
dodec-5-enoyl-[acyl-carrier protein]
0.0537
lauroyl-CoA
-
wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C
0.0082
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.0055 - 0.51
malonyl-CoA
0.59
malonyl-phosphopantetheine
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0061
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0062
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0237
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.0139
myristoyl-[acyl-carrier protein]
-
-
0.04 - 0.216
palmitoleoyl-[acyl-carrier protein]
0.0036
palmitoyl-[acyl-carrier protein]
-
-
0.043 - 0.06
tetradec-7-enoyl-[acyl-carrier protein]
0.047 - 0.068
tetradecanoyl-[acyl-carrier protein]
0.024
dodec-5-enoyl-[acyl-carrier protein]
37°C
0.024
dodec-5-enoyl-[acyl-carrier protein]
27°C
0.0055
malonyl-CoA
-
-
0.0283
malonyl-CoA
-
R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C
0.51
malonyl-CoA
-
wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C
0.04
palmitoleoyl-[acyl-carrier protein]
pH 7.2
0.097
palmitoleoyl-[acyl-carrier protein]
27°C
0.216
palmitoleoyl-[acyl-carrier protein]
37°C
0.043
tetradec-7-enoyl-[acyl-carrier protein]
27°C
0.06
tetradec-7-enoyl-[acyl-carrier protein]
37°C
0.047
tetradecanoyl-[acyl-carrier protein]
27°C
0.068
tetradecanoyl-[acyl-carrier protein]
37°C
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