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an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
-
-
-
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + CoA
-
-
-
?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
acyl-CoA + [acyl-carrier protein]
acyl-[acyl-carrier protein] + CoA
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
butyryl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
beta-ketohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
ir
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
cis-9-hexadecenoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexadecenoyl-[acyl-carrier protein] + CO2 + CoA
-
-
-
-
?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
i.e. palmitoyl-[acyl-carrier-protein]
-
-
?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
malonyl-ACP + lauroyl-ACP
?
-
-
-
-
?
malonyl-ACP + lauroyl-CoA
?
-
-
-
-
?
Malonyl-CoA
Acetyl-CoA + CO2
-
decarboxylation reaction
-
-
?
malonyl-CoA + lauroyl-ACP
?
-
-
-
-
?
malonyl-phosphopantetheine-14-mer + lauroyl-ACP
?
-
-
-
-
?
malonyl-phosphopantetheine-16-mer + lauroyl-ACP
?
-
-
-
-
?
malonyl-phosphopantetheine-8-mer + lauroyl-ACP
?
-
-
-
-
?
malonyl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + CO2
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
propionyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
beta-ketopentanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
ir
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
additional information
?
-
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
ir
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
r
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
r
acyl-CoA + [acyl-carrier protein]
acyl-[acyl-carrier protein] + CoA
-
tetradecanoyl-CoA and cis-9-hexadecenoyl-CoA are poor substrates
-
r
acyl-CoA + [acyl-carrier protein]
acyl-[acyl-carrier protein] + CoA
-
catalyzes fatty acyl transfer between CoA and [acyl-carrier-protein], but no direct transfer to the enzyme as with acyl-[acyl-carrier-protein]
-
-
?
acyl-CoA + [acyl-carrier protein]
acyl-[acyl-carrier protein] + CoA
-
catalyzes fatty acyl transfer between CoA and [acyl-carrier-protein], but no direct transfer to the enzyme as with acyl-[acyl-carrier-protein]
-
r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
part of non-associated fatty acid synthase system of plants and prokaryotes
-
-
?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
part of non-associated fatty acid synthase system of plants and prokaryotes
-
-
ir
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
part of non-associated fatty acid synthase system of plants and prokaryotes
-
-
r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
involved in biosynthesis of saturated fatty acids
-
-
ir
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
involved in biosynthesis of saturated fatty acids
-
-
r
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
involved in biosynthesis of unsaturated and saturated fatty acids
-
-
?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
responsible for chain elongation during de novo fatty acid synthesis
-
-
?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
involved in biosynthesis of mono-unsaturated long-chain fatty acids
-
-
?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
-
-
-
-
?
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
-
key step in the unsaturated fatty acid, UFA, synthesis pathway. FabB is negatively regulated by the FabR protein
the product is not incorporated into the complex lipids of the bacterium
-
?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
r
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
poor substrate, synthase I
-
-
?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
poor substrate, synthase I
-
-
r
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
best substrate, synthase II
-
-
?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
best substrate, synthase II
-
-
r
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
not cis-vaccenoyl-[acyl-carrier-protein], i.e. cis-11-octenoyl-[acyl-carrier-protein]
-
-
?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
not cis-vaccenoyl-[acyl-carrier-protein], i.e. cis-11-octenoyl-[acyl-carrier-protein]
-
-
r
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
from C-10 to C-16, e.g. cis-5-decenoyl-[acyl-carrier-protein], cis-5-dodecenoyl-[acyl-carrier-protein], cis-7-tetradecenoyl-[acyl-carrier-protein], cis-9-hexenoyl-[acyl-carrier-protein], i.e. palmitoleoyl-[acyl-carrier-protein], poor substrates
-
-
?
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
from C-10 to C-16, e.g. cis-5-decenoyl-[acyl-carrier-protein], cis-5-dodecenoyl-[acyl-carrier-protein], cis-7-tetradecenoyl-[acyl-carrier-protein], cis-9-hexenoyl-[acyl-carrier-protein], i.e. palmitoleoyl-[acyl-carrier-protein], poor substrates
-
-
r
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
ir
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
r
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
characterization of hexanoyl-enzyme intermediate
-
-
r
malonyl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + CO2
-
catalyzes malonyl-[acyl-carrier-protein] decarboxylation independent of fatty acyl-[acyl-carrier-protein]
-
?
malonyl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + CO2
-
decarboxylation with 2-3% the rate of beta-ketoacyl-[acyl-carrier-protein]-synthesis
-
?
malonyl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + CO2
-
wild-type synthase I and mutants C163A and C163S
-
?
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
ir
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
ir
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
substrate specificity, overview
-
r
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
not hexadecanoyl-[acyl-carrier-protein]
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
not hexadecanoyl-[acyl-carrier-protein]
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
specific for acyl-[acyl-carrier-protein] thioesters, not acyl-CoA or acyl pantetheine thioesters
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
specific for acyl-[acyl-carrier-protein] thioesters, not acyl-CoA or acyl pantetheine thioesters
-
?
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
fatty acid composition of Brassica napus wild-type and transgenic plants overexpressing the E. coli synthase III
-
?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
-
-
-
?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
poor substrate
-
-
r
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
synthase I
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme also catalyzes a malonyl-CoA-CO2 exchange reaction, overview: substrates and kinetics
-
-
?
additional information
?
-
-
synthase I and II have nearly the same substrate specificity
-
-
?
additional information
?
-
-
enzyme active site structure of wild-type and mutants with or without bound C12 or C8, overview
-
-
?
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acyl-CoA
-
at high concentrations
genistein
5,7-dihydroxy-3-(4-hydroxyphenyl)chromen-4-one
isorhamnetin
3,5,7-trihydroxy-2-(4-hydroxy-3-methoxyphenyl)chromen-4-one
N-(3-pyridinyl)-hexanamide
result of an in silicio screening, antimicrobial activity, binding to beta-ketoacyl-[acyl-carrier-protein] synthase I characterized by saturation-transfer difference NMR spectroscopy
thiolactomicin
thiolactomycin is an inhibitor of KAS I and inhibits bacterial cell growth through inhibition of the beta-ketoacyl-ACP synthase activity of type II fatty acids ynthases
Urea
-
about 50% inhibition at 1 M, complete inactivation at 4 M
[Acyl-carrier-protein]
-
wild-type synthase I and mutants, not mutants C163S and K328A, overview
cerulenin
-
-
cerulenin
-
analysis of the binding mechanism, mimicks the condensation transition state
cerulenin
-
FabB: inhibition is irreversible
cerulenin
forms two hydrogen bonding interactions with H333 and backbone amide hydrogen of G391 and a hydrophobic interaction with M197, F229, and F231
cerulenin
irreversible inhibitor of beta-ketoacyl-ACP synthases I and II but is not a selective anti-bacterial because it is also a potent inhibitor of the condensation reaction catalyzed by the mammalian multifunctional (type I) fatty-acidsynthase
iodoacetamide
-
-
iodoacetamide
-
no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation
iodoacetamide
-
synthase I and II
iodoacetamide
-
after incubation with 2-mercaptethanol
iodoacetamide
-
acyl-[acyl-carrier-protein]-derivatives, e.g. acetyl-[acyl-carrier-protein], hexanoyl-CoA, octanoyl-CoA, decanoyl-CoA protect
N-ethylmaleimide
-
-
N-ethylmaleimide
-
after incubation with 2-mercaptoethanol
N-ethylmaleimide
-
no inhibition of malonyl-[acyl-carrier-protein]-decarboxylation
N-ethylmaleimide
-
acyl-[acyl-carrier-protein]-derivatives protect
thiolactomycin
-
thiolactomycin
-
synthase III
thiolactomycin
-
FabB: inhibition is reversible, competitive
thiolactomycin
-
analysis of the binding mechanism, mimics malonyl-[acyl-carrier-protein]
thiolactomycin
forms a hydrogen bonding with H333 and a hydrophobic interaction of Phe229 and Thr300 with ecKAS I
additional information
-
inhibitor screening of 250000 synthetic compounds, enzyme-inhibitor binding study by NMR spectroscopy, three-dimensional structure of ecKAS I with inhibitors, overview. No or poor inhibition by 2-(2-methylanilino)-N'-[(E)-(6-methylpyridin-2-yl)methylidene]propanehydrazide, (5Z)-5-([4-[(propan-2-yl)oxy]phenyl]methylidene)-3-(prop-2-en-1-yl)-1,3-thiazolidine-2,4-dione, 1-[2-[4-(2-ethoxyethyl)piperazin-1-yl]-2-oxoethyl]pyrrolidin-2-one, 2-(hexylcarbamoyl)cyclohexane-1-carboxylic acid, 2-[(4-methylbenzene-1-sulfonyl)methyl]prop-2-enamide, 2-([(E)-[(3-nitrophenyl)methylidene]amino]oxy)propanoic acid, 2-[4-(furan-2-yl)phenoxy]-2-methylpropanoic acid, and N-(3-pyridinyl) hexanamide, the latter is though active against Staphylococcus aureus and Enterococcus faecalis
-
additional information
inhibitor screening of 250000 synthetic compounds, enzyme-inhibitor binding study by NMR spectroscopy, three-dimensional structure of ecKAS I with inhibitors, overview. No or poor inhibition by 2-(2-methylanilino)-N'-[(E)-(6-methylpyridin-2-yl)methylidene]propanehydrazide, (5Z)-5-([4-[(propan-2-yl)oxy]phenyl]methylidene)-3-(prop-2-en-1-yl)-1,3-thiazolidine-2,4-dione, 1-[2-[4-(2-ethoxyethyl)piperazin-1-yl]-2-oxoethyl]pyrrolidin-2-one, 2-(hexylcarbamoyl)cyclohexane-1-carboxylic acid, 2-[(4-methylbenzene-1-sulfonyl)methyl]prop-2-enamide, 2-([(E)-[(3-nitrophenyl)methylidene]amino]oxy)propanoic acid, 2-[4-(furan-2-yl)phenoxy]-2-methylpropanoic acid, and N-(3-pyridinyl) hexanamide, the latter is though active against Staphylococcus aureus and Enterococcus faecalis
-
additional information
screening of 50 flavonoids for inhibition potency against the enzyme, in silico molecular docking study, overview. Only genistein and isorhamnetin show inhibition as well as drug likeliness and bioavailability obeying the Lipinski's guidelines of five. No or poor effects by daidzein, luteolin, herbacetin, petunidin, herbacetin, malvidin, casticin, pinocembrin, kaempferol, butin, 7,3',4',5'-tetramethoxyflavanone, sternbin, galangin, dihydrooroxylin, naringenin, hispidulin, prunetin, 3,6-dihydroxyflavone, tricin, hesperetin, dihydroechioidinin 5,7-dihydroxytrimethoxyflavanone, liquiritigenin, diosmetin, isosakuranetin, dihydrowogonin, syringetin, chrysin, cajanin, naringenin trimethyl ether, pectolinarigenin, 3',4',5',5,7-pentamethoxyflavanone, glycitein, tectorigenin, 4'-hydroxy-5,6,7-trimethoxyflavanone, naringenin 5-methyl ether, 6,2',4'-trimethoxyflavanone, naringenin 7,4'-dimethyl ether, 7-hydroxyflavanone, 5,7-dihydroxyisoflavone, onysilin, and biochanin A
-
additional information
-
screening of 50 flavonoids for inhibition potency against the enzyme, in silico molecular docking study, overview. Only genistein and isorhamnetin show inhibition as well as drug likeliness and bioavailability obeying the Lipinski's guidelines of five. No or poor effects by daidzein, luteolin, herbacetin, petunidin, herbacetin, malvidin, casticin, pinocembrin, kaempferol, butin, 7,3',4',5'-tetramethoxyflavanone, sternbin, galangin, dihydrooroxylin, naringenin, hispidulin, prunetin, 3,6-dihydroxyflavone, tricin, hesperetin, dihydroechioidinin 5,7-dihydroxytrimethoxyflavanone, liquiritigenin, diosmetin, isosakuranetin, dihydrowogonin, syringetin, chrysin, cajanin, naringenin trimethyl ether, pectolinarigenin, 3',4',5',5,7-pentamethoxyflavanone, glycitein, tectorigenin, 4'-hydroxy-5,6,7-trimethoxyflavanone, naringenin 5-methyl ether, 6,2',4'-trimethoxyflavanone, naringenin 7,4'-dimethyl ether, 7-hydroxyflavanone, 5,7-dihydroxyisoflavone, onysilin, and biochanin A
-
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.
0.019 - 0.04
acetyl-[acyl-carrier protein]
0.012 - 0.014
cis-3-decenoyl-[acyl-carrier protein]
0.017 - 0.138
cis-9-hexadecenoyl-[acyl-carrier protein]
0.0032 - 0.06
lauroyl-ACP
0.0586
lauroyl-CoA
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C
0.0115
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.153
malonyl-CoA
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.0158
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.029
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.0142
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.025
malonyl-[acyl-carrier protein]
-
pH 7.0
additional information
additional information
-
0.019
acetyl-[acyl-carrier protein]
-
pH 7.0
0.031
acetyl-[acyl-carrier protein]
-
synthase I
0.04
acetyl-[acyl-carrier protein]
-
synthase II
0.04
acetyl-[acyl-carrier protein]
-
acyl-carrier-protein, fatty acyl transfer between tetradecanoyl-CoA and acyl-carrier-protein
0.012
cis-3-decenoyl-[acyl-carrier protein]
-
synthase I
0.014
cis-3-decenoyl-[acyl-carrier protein]
-
synthase II
0.017
cis-9-hexadecenoyl-[acyl-carrier protein]
-
synthase II
0.138
cis-9-hexadecenoyl-[acyl-carrier protein]
-
synthase I
0.0032
lauroyl-ACP
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C
0.0039
lauroyl-ACP
-
wild type protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C
0.0067
lauroyl-ACP
-
K151Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C
0.05
lauroyl-ACP
-
R62Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C
0.056
lauroyl-ACP
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R66Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C
0.06
lauroyl-ACP
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K63Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C
additional information
additional information
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additional information
additional information
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additional information
additional information
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kinetic data of synthase I and II at different temperatures with various substrates
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C163A
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synthase I, site-directed mutagenesis, active site mutant, no activity, but decarboxylates malonyl-[acyl-carrier-protein]
C163S
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synthase I, site-directed mutagenesis, active site mutant, increased activity, decarboxylates malonyl-[acyl-carrier-protein]
D306A
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synthase I, site-directed mutagenesis, active site mutant, increased activity
E309A
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synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298A
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synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298E
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site-directed mutagenesis, the mutant is decarboxylation deficient, residual decarboxylase activity in the range of pH 6.08.0, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H298Q
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site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H333A
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synthase I, site-directed mutagenesis, active site mutant, increased activity
K151Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
K328E
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site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328F
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site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328H
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site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328I
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site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328R
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site-directed mutagenesis, the mutant is almost completely decarboxylation deficient, crystal structure determination with the free mutant enzyme, comparison to the wild-type enzyme structure
K63Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R62Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R66Q
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conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
K328A
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synthase I, site-directed mutagenesis, active site mutant, reduced activity
K328A
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site-directed mutagenesis, the mutant is completely decarboxylation deficient, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
additional information
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transformation of Brassica napus via Agrobacterium tumefaciens infection with binary vector overexpressing Escherichia coli fabH gene, targeted expression in cytoplasm and plastids is seed specific, modified fatty acid profile of seed oil
additional information
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introduction of temperature-sensitive mutation in fabB into strain K27 by phage P1-mediated transduction using closely linked Tn10 insertion as selectable marker. A fabB mutant strain accumulates less cis-5-dodecenoic acid than the parental wild-type strain. The wild-type strain also accumulates 2.7fold more cis-7-tetradecenoate than the fabB(Ts) strain. The combination of null mutations in fadD and fabA or fabB is synthetically lethal even in the presence of oleic acid supplementation. A temperature-sensitive mutation is used rather than null mutations because a strain having fabB null mutation has an obligate requirement for an unsaturated fatty acid and FabD is required for uptake of the supplement
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Vagelos, R.P.
Acyl group transfer (acyl carrier protein)
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
8
155-199
1973
Clostridium kluyveri, Escherichia coli
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Acyl carrier protein
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Escherichia coli, Escherichia coli B / ATCC 11303
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27
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Brassica napus, Escherichia coli
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beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis
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Bacillus subtilis, Escherichia coli
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Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)
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276
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Escherichia coli, Haemophilus influenzae, Streptococcus pneumoniae (P0A3C5)
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Price, A.C.; Choi, K.H.; Heath, R.J.; Li, Z.; White, S.W.; Rock, C.O.
Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism
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276
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2001
Escherichia coli
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McGuire, K.A.; Siggaard-Andersen, M.; Bangera, M.G.; Olsen, J.G.; von Wettstein-Knowles, P.
beta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket
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40
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2001
Escherichia coli
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Kursula, P.; Sikkilae, H.; Fukao, T.; Kondo, N.; Wierenga, R.K.
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Escherichia coli (P0A953), Escherichia coli
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A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes
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52
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2003
Escherichia coli
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von Wettstein-Knowles, P.; Olsen, J.G.; McGuire, K.A.; Henriksen, A.
Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases
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273
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Escherichia coli
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284
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Substrate recognition by beta-ketoacyl-ACP synthases
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50
10678-10686
2011
Escherichia coli, Mycobacterium tuberculosis
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In silico screening of a novel inhibitor of beta-ketoacyl acyl carrier protein synthase i
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32
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2011
Escherichia coli, Escherichia coli (E2QPI4)
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Sabbagh, G.; Berakdar, N.
Docking studies of flavonoid compounds as inhibitors of beta-ketoacyl acyl carrier protein synthase I (Kas I) of Escherichia coli
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61
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Escherichia coli (P0A953)
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