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Information on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I and Organism(s) Escherichia coli and UniProt Accession P0A953

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EC Tree
IUBMB Comments
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) . The substrate specificity is very similar to that of EC 2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
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Escherichia coli
UNIPROT: P0A953
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
condensing enzyme, beta-ketoacyl synthase, kas i, beta-ketoacyl-acp synthase, beta-ketoacyl synthetase, 3-ketoacyl-acyl carrier protein synthase, 3-ketoacyl-acp synthase, beta-ketoacyl-acp synthase i, beta-ketoacyl-acyl carrier protein synthase i, fatty acid condensing enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-ketoacyl ACP synthase I
-
beta-ketoacyl-ACP-synthase I
-
3-ketoacyl-ACP synthase
-
-
3-ketoacyl-acyl carrier protein synthase
-
-
-
-
3-oxoacyl-[acyl-carrier-protein] synthase
-
-
-
-
acyl-malonyl(acyl-carrier-protein)-condensing enzyme
-
-
-
-
beta-ketoacyl acyl carrier protein synthase
-
-
-
-
beta-ketoacyl acyl carrier protein synthase I
-
beta-ketoacyl synthetase
-
-
-
-
beta-ketoacyl-ACP synthase I
-
-
beta-ketoacyl-ACP synthetase
-
-
-
-
beta-ketoacyl-acyl carrier protein synthetase
-
-
-
-
beta-ketoacyl-[acyl carrier protein] synthase
-
-
-
-
beta-ketoacyl-[acyl-carrier-protein] synthase I
-
-
beta-ketoacylsynthase
-
-
-
-
condensing enzyme
-
-
-
-
Cys-His-His-type beta-ketoacyl-acyl carrier protein synthase
-
-
fatty acid condensing enzyme
-
-
-
-
KAS I
synthase, 3-oxoacyl-[acyl-carrier-protein]
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
catalytic active site residues are Cys163 and His333, the active site contains two oxyanion holes, stabilizing the thioester oxyanion of acetylated CoA and of acetylated Cys92, respectively
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
Acyl group transfer
-
-
-
-
Claisen condensation
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-[acyl-carrier protein]:malonyl-[acyl-carrier protein] C-acyltransferase (decarboxylating)
This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16) [4]. The substrate specificity is very similar to that of EC 2.3.1.179, beta-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Delta9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature [4,5].
CAS REGISTRY NUMBER
COMMENTARY hide
9077-10-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
-
-
-
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
-
-
-
?
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
acyl-CoA + [acyl-carrier protein]
acyl-[acyl-carrier protein] + CoA
show the reaction diagram
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
butyryl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
beta-ketohexanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
ir
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
show the reaction diagram
cis-9-hexadecenoyl-CoA + malonyl-[acyl-carrier protein]
3-oxo-hexadecenoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
-
-
-
-
?
cis-9-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-11-octadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
cis-mono-unsaturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
cis-mono-unsaturated 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
decanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
dodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
dodecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxotetradecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
hexadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
i.e. palmitoyl-[acyl-carrier-protein]
-
-
?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
malonyl-ACP + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-ACP + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
Malonyl-CoA
Acetyl-CoA + CO2
show the reaction diagram
-
decarboxylation reaction
-
-
?
malonyl-CoA + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-14-mer + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-16-mer + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-8-mer + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
octanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
propionyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
beta-ketopentanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
ir
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein]
show the reaction diagram
-
-
-
?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
cis-3-decenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-cis-5-dodecenoyl-[acyl-carrier protein] + acyl-carrier protein
show the reaction diagram
-
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
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,6-dihydroxyflavone
-
acetyl-CoA
-
-
acyl-CoA
-
at high concentrations
cerulenin
genistein
5,7-dihydroxy-3-(4-hydroxyphenyl)chromen-4-one
homoeriodictyol
-
iodoacetamide
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
N-ethylmaleimide
SB418011
-
-
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
thiolactomycin
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
dithiothreitol
phosphate
-
activation, 0.2 M
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 0.083
lauroyl-ACP
0.073
lauroyl-CoA
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C
0.011
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.12
malonyl-CoA
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.04
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.11
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.018
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83 - 18.3
lauroyl-ACP
1.27
lauroyl-CoA
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C
10
malonyl-ACP
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
0.78
malonyl-CoA
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
3
malonyl-phosphopantetheine-14-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
3.8
malonyl-phosphopantetheine-16-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
1.3
malonyl-phosphopantetheine-8-mer
-
wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.403
-
purified enzyme
3.81
-
purified enzyme
5.5
-
synthase I
6.3
-
synthase II
7.5
-
purified synthase II
9
-
purified synthase I
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.1
-
synthase II
7.2
-
synthase I
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 7.6
-
synthase II, about half-maximal activity at pH 5.2 and pH 7.6
6.3 - 8
-
synthase I, about half-maximal activity at pH 6.3 and pH 8.0
6.5 - 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
22
-
assay at room temperature
27
-
assay at
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
-
2 * 34000, SDS-PAGE
35000
-
2 * 35000, SDS-PAGE
37000
-
2 * 37000, gel filtration after 6 M guanidinium chloride treatment
66000
67600
-
gel filtration
76000
-
synthase II, gel filtration
80000
-
synthase I, sedimentation equilibrium method
85000
-
synthase II, sedimentation equilibrium method
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of crystal structures of the active sites of Escherichia coli KAS I with human cytosolic acetoacetyl-CoA thiolase and bacterial thiolase, overview
in complex with Escherichia coli acyl-carrier protein, sitting drop vapor diffusion method, using 0.1 M sodium acetate pH 5.4, 0.2 M ammonium acetate, and 20% (w/v) PEG 4000
purified recombinant wild-type and mutant enzymes, free or bound to C8 and C12, respectively, X-ray diffraction structure determination and analysis at 1.8-2.4 A resolution
-
structure analysis, three-dimensional model of enzyme complexed with inhibitors thiolactomycin and cerulenin
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C163A
-
synthase I, site-directed mutagenesis, active site mutant, no activity, but decarboxylates malonyl-[acyl-carrier-protein]
C163S
-
synthase I, site-directed mutagenesis, active site mutant, increased activity, decarboxylates malonyl-[acyl-carrier-protein]
D306A
-
synthase I, site-directed mutagenesis, active site mutant, increased activity
E309A
-
synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298A
-
synthase I, site-directed mutagenesis, active site mutant, reduced activity
H298E
-
site-directed mutagenesis, the mutant is decarboxylation deficient, residual decarboxylase activity in the range of pH 6.0–8.0, crystal structure determination with the mutant enzyme free or bound to C12, comparison to the wild-type enzyme structure
H298Q
-
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
-
synthase I, site-directed mutagenesis, active site mutant, increased activity
K151Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
K328A
K328E
-
site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328F
-
site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328H
-
site-directed mutagenesis, the mutant is completely decarboxylation deficient
K328I
-
site-directed mutagenesis, the mutant is almost completely decarboxylation deficient
K328R
-
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
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R62Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
R66Q
-
conserved between FabB, FabF and KasA, proposed to be important for ACP recognition
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
inactivation after 1 min
43
-
t1/2 synthase I: 18 min, t1/2 synthase II: 81 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
EDTA stabilizes
-
unstable during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation by formic acid
-
486918
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 90% loss of activity within 1 year
-
-20°C, at least 1 month
-
-20°C, complete loss of activity in the presence of EDTA and 2-mercaptoethanol
-
-20°C, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography
immobilized metal ion affinity chromatography
immobilized metal ion affinity chromatography (Ni2+)
-
isolation of hexanoyl-enzyme intermediate complex
-
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant synthase I and mutants as His-tagged protein from E. coli
-
recombinant synthases I, i.e. FabA, II, i.e. FabB, and III, i.e.FabH
-
synthases I and II
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression of synthase I and mutants as His-tagged proteins in Escherichia coli
-
His-tagged protein expressed in Escherichia coli BL21(DE3)
His-tagged protein expressed in Escherichia coli pLysS
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
synthase III, overexpression in Escherichia coli strain JM101, construction of binary expression vectors for transformation of Brassica napus
-
synthases I, II, and III, recombinant expression
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
Prescott, D.J.; Vagelos, P.R.
Acyl carrier protein
Adv. Enzymol. Relat. Areas Mol. Biol.
36
269-311
1972
Escherichia coli
Manually annotated by BRENDA team
Toomey, R.E.; Wakil, S.J.
Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli
J. Biol. Chem.
241
1159-1165
1966
Escherichia coli
Manually annotated by BRENDA team
Alberts, A.W.; Majerus, P.W.; Vagelos, P.R.
beta-Ketoacyl acyl carrier protein synthase
Methods Enzymol.
14
57-60
1969
Escherichia coli
-
Manually annotated by BRENDA team
Garwin, J.L.; Klages, A.L.; Cronan, J.E.
Structural, enzymatic, and genetic studies of beta-ketoacyl-acyl carrier protein synthases I and II of Escherichia coli
J. Biol. Chem.
255
11949-11956
1980
Escherichia coli
Manually annotated by BRENDA team
Alberts, A.W.; Bell, R.M.; Vagelos, P.R.
Acyl carrier protein. XV. Studies of beta-ketoacyl-acyl carrier protein synthetase
J. Biol. Chem.
247
3190-3198
1972
Escherichia coli
Manually annotated by BRENDA team
D'Agnolo, G.; Rosenfeld, I.S.; Vagelos, P.R.
beta-Ketoacyl-acyl carrier protein synthetase. Characterization of the acyl-enzyme intermediate
J. Biol. Chem.
250
5283-5288
1975
Escherichia coli
Manually annotated by BRENDA team
D'Agnolo, G.; Rosenfeld, I.S.; Vagelos, P.R.
Multiple forms of beta-ketoacyl-acyl carrier protein synthetase in Escherichia coli
J. Biol. Chem.
250
5289-5294
1975
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Verwoert, I.I.G.S.; van der Linden, K.H.; Walsh, M.C.; Nijkamp, H.J.J.; Stuitje, A.R.
Modification of Brassica napus seed oil by expression of the Escherichia coli fabH gene, encoding 3-ketoacyl-acyl carrier protein synthase III
Plant Mol. Biol.
27
875-886
1995
Brassica napus, Escherichia coli
Manually annotated by BRENDA team
Choi, K.H.; Heath, R.J.; Rock, C.O.
beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis
J. Bacteriol.
182
365-370
2000
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Khandekar, S.S.; Gentry, D.R.; Van Aller, G.S.; Warren, P.; Xiang, H.; Silverman, C.; Doyle, M.L.; Chambers, P.A.; Konstantinidis, A.K.; Brandt, M.; Daines, R.A.; Lonsdale, J.T.
Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH)
J. Biol. Chem.
276
30024-30030
2001
Escherichia coli, Haemophilus influenzae, Streptococcus pneumoniae (P0A3C5)
Manually annotated by BRENDA team
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
J. Biol. Chem.
276
6551-6559
2001
Escherichia coli
Manually annotated by BRENDA team
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
Biochemistry
40
9836-9845
2001
Escherichia coli
Manually annotated by BRENDA team
Kursula, P.; Sikkilae, H.; Fukao, T.; Kondo, N.; Wierenga, R.K.
High resolution crystal structures of human cytosolic thiolase (CT): A comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I
J. Mol. Biol.
347
189-201
2005
Escherichia coli (P0A953), Escherichia coli
Manually annotated by BRENDA team
Dawe, J.H.; Porter, C.T.; Thornton, J.M.; Tabor, A.B.
A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes
Proteins
52
427-435
2003
Escherichia coli
Manually annotated by BRENDA team
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
FEBS J.
273
695-710
2006
Escherichia coli
Manually annotated by BRENDA team
Feng, Y.; Cronan, J.E.
Escherichia coli unsaturated fatty acid synthesis: complex transcription of the fabA gene and in vivo identification of the essential reaction catalyzed by FabB
J. Biol. Chem.
284
29526-29535
2009
Escherichia coli
Manually annotated by BRENDA team
Borgaro, J.; Chang, A.; MacHutta, C.; Zhang, X.; Tonge, P.
Substrate recognition by beta-ketoacyl-ACP synthases
Biochemistry
50
10678-10686
2011
Escherichia coli, Mycobacterium tuberculosis
Manually annotated by BRENDA team
Lee, J.; Jeong, K.; Lee, J.; Kang, D.; Kim, Y.
In silico screening of a novel inhibitor of beta-ketoacyl acyl carrier protein synthase i
Bull. Korean Chem. Soc.
32
1645-1649
2011
Escherichia coli, Escherichia coli (E2QPI4)
-
Manually annotated by BRENDA team
Sabbagh, G.; Berakdar, N.
Docking studies of flavonoid compounds as inhibitors of beta-ketoacyl acyl carrier protein synthase I (Kas I) of Escherichia coli
J. Mol. Graph. Model.
61
214-223
2015
Escherichia coli (E2QPI4), Escherichia coli
Manually annotated by BRENDA team
Milligan, J.C.; Lee, D.J.; Jackson, D.R.; Schaub, A.J.; Beld, J.; Barajas, J.F.; Hale, J.J.; Luo, R.; Burkart, M.D.; Tsai, S.C.
Molecular basis for interactions between an acyl carrier protein and a ketosynthase
Nat. Chem. Biol.
15
669-671
2019
Escherichia coli (P0A953)
Manually annotated by BRENDA team