Information on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.1.41
-
RECOMMENDED NAME
GeneOntology No.
beta-ketoacyl-[acyl-carrier-protein] synthase I
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
Claisen condensation
condensation
decarboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5Z)-dodec-5-enoate biosynthesis
-
-
8-amino-7-oxononanoate biosynthesis I
-
-
arachidonate biosynthesis
-
-
Biotin metabolism
-
-
Fatty acid biosynthesis
-
-
fatty acid biosynthesis initiation II
-
-
fatty acid biosynthesis initiation III
-
-
fatty acid elongation -- saturated
-
-
gondoate biosynthesis (anaerobic)
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
mycolate biosynthesis
-
-
octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
-
-
oleate biosynthesis IV (anaerobic)
-
-
palmitate biosynthesis
-
-
palmitate biosynthesis I (animals and fungi)
-
-
palmitate biosynthesis II (bacteria and plants)
-
-
palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate)
-
-
stearate biosynthesis II (bacteria and plants)
-
-
stearate biosynthesis III (fungi)
-
-
superpathway of fatty acid biosynthesis initiation (E. coli)
-
-
superpathway of mycolate biosynthesis
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
synthase II
-
-
Manually annotated by BRENDA team
genes fabH1 and fabH2, 2 synthase III isozymes
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
safflower
-
-
Manually annotated by BRENDA team
seed plastid-specific isoform with similarities to synthase I type
-
-
Manually annotated by BRENDA team
synthase IV
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Z
-
-
Manually annotated by BRENDA team
Z
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Bonus
-
-
Manually annotated by BRENDA team
sp. lactis IL1403
-
-
Manually annotated by BRENDA team
synthase I, i.e. KasA
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
FabF/FabH; strain 3D7, gene fabBF, encoding the only elongating beta-ketoacyl-ACP synthase in the organism
-
-
Manually annotated by BRENDA team
synthase III, gene fabH
-
-
Manually annotated by BRENDA team
synthase III-like activity
-
-
Manually annotated by BRENDA team
mitochondrial beta-ketoacyl synthase; ssp. brucei, strain 427, procyclic trypanosomes
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
FabB catalyzes the elongation of cis-3-decenoyl-ACP produced by FabA to generate the first 12-carbon cis-unsaturated fatty acid intermediate, 3-oxo-cis-5-decenoyl-ACP, which is converted to cis-5-dodecenoyl-ACP. FabB is essential in the unsaturated fatty acid, UFA, synthesis pathway, strains lacking FabB are UFA auxotroph, overview. FabB cannot be substituted by FabF
physiological function
crucial for fatty acid synthesis, deficiency results in semidwarf and variegated leaves, in a mutant chloroplast division is arrested at early developmental stages of rosette leaves
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-6-octadecenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
acetyl-CoA + malonyl-CoA
3-oxobutyryl-CoA + CoA
show the reaction diagram
-
-
formation of about 1% triacetic acid lactone
-
?
acetyl-CoA + malonyl-[acyl-carrier protein]
acetoacyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
butanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexanoyl-[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
C10-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
C12-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
C12-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
C14-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
C14-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
C16-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
C4-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
C6-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
C6-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
C8-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
best substrate
-
-
?
C8-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
C10-[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
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-ACP + malonyl-ACP
?
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
eicosanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxodocosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
hexadecanoyl-CoA + malonyl-[acyl-carrier protein]
3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + CoA
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
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
isobutyryl-CoA + malonyl-[acyl-carrier protein]
?
show the reaction diagram
malonyl-ACP + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-ACP + lauroyl-CoA
?
show the reaction diagram
-
-
-
-
?
malonyl-ACP + palmitoyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-ACP + palmitoyl-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-CoA + palmitoyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-14-mer + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-14-mer + palmitoyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-16-mer + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-16-mer + palmitoyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-8-mer + lauroyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-phosphopantetheine-8-mer + palmitoyl-ACP
?
show the reaction diagram
-
-
-
-
?
malonyl-[acyl-carrier protein]
acetyl-[acyl-carrier protein] + CO2
show the reaction diagram
malonyl-[acyl-carrier protein] + lauroyl-CoA
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
malonyl-[acyl-carrier protein] + myristoyl-CoA
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
malonyl-[acyl-carrier protein] + palmitoyl-CoA
? + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
myristoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
octadecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoeicosanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
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
palmitoyl-[acyl-carrier protein] + malonyl-CoA
3-oxostearoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
-
-
-
-
?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
palmitoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[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
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
stearoyl-[acyl-carrier protein] + malonyl-CoA
3-oxoeicosanoyl-[acyl-carrier protein] + CO2 + CoA
show the reaction diagram
-
only in sheath epidermis
-
-
?
tetradecanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxohexadecanoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hexadecenoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxo-6-octadecenoyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
reaction is part of petroselinic acid biosynthesis, synthase IV
-
-
?
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
acyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
-
-
-
?
an acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
a 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
show the reaction diagram
-
the endoplasmic reticulum enzyme is involved in synthesis of very 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
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
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-one
i.e. HR19; strong, synthase III
5-chloro-4-phenyl-[1,2]-dithiol-3-one
complete inhibition at 0.01 nM, synthase III; i.e. HR12
acetyl-CoA
-
-
acyl-CoA
-
at high concentrations
arsenite
Butyryl-CoA
-
synthase III mutants C122Aand C122Q: inhibition of decarboxylation activity in presence of
C75
-
a synthetic inhibitor of fatty acid synthase, inhibits also the beta-ketoacyl synthase, not in simple first order rate reaction, C75 is a competitive, irreversible inhibitor of the overall reaction, the beta-ketoacyl synthase activity and the enoyl reductase activity substrates do not protect the thioesterase activity of rat liver FAS from inactivation by C75, but malonyl-CoA and acetyl-CoA protect the FAS beta-ketoacyl synthase reaction from inactivation by C75 in a competitive manner, overview
cerulenin
iodoacetamide
isobutyryl-CoA
-
synthase III mutants C122Aand C122Q: inhibition of decarboxylation activity in presence of
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
p-chloromercuribenzoate
-
complete inhibition at 1 mM
palmitoyl-CoA
-
substrate inhibition above 0.003 mM
platencin
-
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, purified FabH IC50: 0.016 mM, overview
SB418011
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
0.0024 - 0.0403
acetyl-CoA
0.019 - 0.05
acetyl-[acyl-carrier protein]
0.0039
butanoyl-[acyl-carrier protein]
-
pH 6.8, 37C
0.00071 - 0.0023
Butyryl-CoA
0.403
C10-[acyl-carrier protein]
-
pH 7.5, 37C, recombinant enzyme
0.196
C12-[acyl-carrier protein]
-
pH 7.5, 37C, recombinant enzyme
0.437
C14-[acyl-carrier protein]
-
pH 7.5, 37C, recombinant enzyme
0.211
C4-[acyl-carrier protein]
-
pH 7.5, 37C, recombinant enzyme
0.116
C6-[acyl-carrier protein]
-
pH 7.5, 37C, recombinant enzyme
0.198
C8-[acyl-carrier protein]
-
pH 7.5, 37C, recombinant enzyme
0.012 - 0.014
cis-3-decenoyl-[acyl-carrier protein]
0.017 - 0.138
cis-9-hexadecenoyl-[acyl-carrier protein]
0.0018 - 0.0133
decanoyl-[acyl-carrier protein]
0.0023 - 0.0095
dodecanoyl-[acyl-carrier protein]
0.002 - 0.0025
eicosanoyl-[acyl-carrier protein]
0.0019 - 0.0075
hexanoyl-[acyl-carrier protein]
0.00032 - 0.00041
isobutyryl-CoA
0.0032 - 0.06
lauroyl-ACP
0.0586
Lauroyl-CoA
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25C
0.0058 - 0.0115
malonyl-ACP
0.004 - 0.153
malonyl-CoA
0.0086 - 0.0158
malonyl-phosphopantetheine-14-mer
0.0051 - 0.029
malonyl-phosphopantetheine-16-mer
0.0047 - 0.0142
malonyl-phosphopantetheine-8-mer
0.0037 - 0.025
malonyl-[acyl-carrier protein]
0.0508
myristoyl-[acyl-carrier protein]
-
pH 6.8, 37C
0.0109
octanoyl-[acyl-carrier protein]
-
pH 6.8, 37C
0.0004
palmitoyl-CoA
-
acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 8.5, 25C
0.0014 - 0.0036
palmitoyl-[acyl-carrier protein]
0.0091 - 0.0139
tetradecanoyl-[acyl-carrier protein]
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91.2
butanoyl-[acyl-carrier protein]
Homo sapiens
-
pH 6.8, 37C
1.32
butyryl-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
3.07
C10-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
0.69
C12-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
1.28
C14-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
1.32
C4-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
0.96
C6-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
1.63
C8-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
3.07 - 551
decanoyl-[acyl-carrier protein]
0.69 - 303
dodecanoyl-[acyl-carrier protein]
0.01 - 0.075
eicosanoyl-[acyl-carrier protein]
0.96 - 353
hexanoyl-[acyl-carrier protein]
0.025 - 0.083
lauroyl-ACP
0.073
Lauroyl-CoA
Escherichia coli
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25C
0.011 - 0.47
malonyl-ACP
0.12 - 0.35
malonyl-CoA
0.04 - 0.38
malonyl-phosphopantetheine-14-mer
0.11 - 0.3
malonyl-phosphopantetheine-16-mer
0.018 - 0.35
malonyl-phosphopantetheine-8-mer
0.0233 - 0.08
malonyl-[acyl-carrier protein]
6
myristoyl-[acyl-carrier protein]
Homo sapiens
-
pH 6.8, 37C
1.63 - 66
octanoyl-[acyl-carrier protein]
0.08
palmitoyl-CoA
Mycobacterium tuberculosis
-
acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 8.5, 25C
0.0267 - 0.0883
palmitoyl-[acyl-carrier protein]
1.28
tetradecanoyl-[acyl-carrier protein]
Plasmodium falciparum
-
pH 7.5, 37C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83 - 18.3
lauroyl-ACP
1.27
Lauroyl-CoA
Escherichia coli
-
wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25C
718
10 - 86.7
malonyl-ACP
0.78 - 38.3
malonyl-CoA
3 - 48.3
malonyl-phosphopantetheine-14-mer
3.8 - 60
malonyl-phosphopantetheine-16-mer
1.3 - 75
malonyl-phosphopantetheine-8-mer
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16
C75
-
pH 7.0, 22C, inactivation of the whole reaction of FAS
0.01
thiolactomycin
-
pH 7.5, 37C, recombinant enzyme
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0158
cerulenin
Plasmodium falciparum
-
irreversible inhibition, IC50: 0.0158 mM
0.016
platencin
Staphylococcus aureus
-
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, purified FabH IC50: 0.016 mM, o
0.0236
thiolactomycin
Plasmodium falciparum
-
competitive inhibition, IC50: 0.0236 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000034
substrate palmitoyl-CoA
0.000006
substrate palmitoyl-CoA
0.000032
substrate palmitoyl-[acyl-carrier-protein]
0.000088
substrate palmitoyl-[acyl-carrier-protein]
0.0017
-
substrate hexanoyl-[acyl-carrier protein], pH 7.0, 37C
0.0055
-
substrate octanoyl-[acyl-carrier protein], pH 7.0, 37C
0.0062
-
substrate decanoyl-[acyl-carrier protein], pH 7.0, 37C
0.0072
-
substrate dodecanoyl-[acyl-carrier protein], pH 7.0, 37C
0.0083
-
purified enzyme
0.009
-
substrate eicosanoyl-[acyl-carrier-protein], pH 7.0, 37C
0.0093
-
substrate palmitoyl-[acyl-carrier protein], pH 7.0, 37C
0.0095
-
substrate myristoyl-[acyl-carrier protein], pH 7.0, 37C
0.0104
-
substrate octadecanoyl-[acyl-carrier-protein], pH 7.0, 37C
0.105
-
purified recombinant enzyme with substrate C6-[acyl-carrier-protein]
0.403
-
purified enzyme
0.8
-
purified synthase I
3.81
-
purified enzyme
5.5
-
synthase I
6.3
-
synthase II
7
-
purified native enzyme
7.5
-
purified synthase II
8.04
-
partially purified enzyme
9
-
purified synthase I
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6.1
-
synthase II
6.6 - 7.7
-
synthase III
7
-
assay at
8.1 - 8.5
-
-
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
5.6 - 7.2
-
synthase II, about half-maximal activity at pH 5.6 and pH 7.2
5.8 - 8
synthase III
5.9 - 6.8
-
synthase I, about half-maximal activity at pH 5.9 and pH 6.8
6.3 - 8
-
synthase I, about half-maximal activity at pH 6.3 and pH 8.0
6.5 - 8
6.8 - 9.1
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
27
-
assay at
35
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 42
30-50% activity at 30 and 42C; 30-50% activity at 30 and 42C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low level
Manually annotated by BRENDA team
-
sheath and lamina, and underlying parenchyma
Manually annotated by BRENDA team
-
most abundant
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
also found in 7-d-old seedling, root, flower, young silique, embryos at late cotyledon stage and stalk
Manually annotated by BRENDA team
-
most abundant
Manually annotated by BRENDA team
-
low level
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella abortus (strain 2308)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Burkholderia xenovorans (strain LB400)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Staphylococcus aureus (strain MW2)
Staphylococcus aureus (strain MW2)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
synthase III-like polyketid synthase, gel filtration, amino acid sequence determination
56000
-
synthase I, gel filtration
57500
-
synthase II, gel filtration
60000
synthase III, gel filtration
63000
-
synthase III, gel filtration
70000
-
about, gel filtration
72000
-
recombinant enzyme, gel filtration
76000
-
synthase II, gel filtration
80000
-
synthase I, sedimentation equilibrium method
85000
-
synthase II, sedimentation equilibrium method
86700
-
synthase I, gel filtration
87400
-
synthase II, gel filtration
87800
-
synthase II, gel filtration
118000
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 38000, synthase III-like polyketid synthase, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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
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
-
purified recombinant enzyme free or complexed with acyl-CoA, hanging drop vapour diffusion method, 0.002 ml of protein solution, containing 0.087 mg of protein with or without 4 mM hexanoyl-CoA, mixed with 0.002 ml of reservoir solution containing 24% w/v PEG 3350 and 0.2 M NH4Cl, 5-8 days at room temperature, rod-shaped single crystals, X-ray diffraction structure determination and analysis at 1.6 A resolution, structure modeling
in complex with lauroyl-CoA
-
hanging drop vapour diffusion method, protein solution: 25 mM Tris-HCl, pH 8.0, 300 mM NaCl, 75 mM imidazole, reservoir solution: 0.085 M tri-sodium citrate, 0.17 M ammonium acetate, 22% w/v polyethylene glycol 4000, 15% v/v glycerol as cryo-protectant, 15% w/v 1,2,3-heptanetriol, x-ray structure analysis, three-dimensional model
-
hanging-drop vapour-diffusion method, ammonium sulfate
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43
-
t1/2 synthase I: 18 min, t1/2 synthase II: 81 min
100
-
inactivation after 1 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes
-
dithiothreitol stabilizes
EDTA stabilizes
-
freezing and thawing inactivates
-
glycerol stabilizes
-
proteinase inhibitors stabilize during purification
-
Triton X-100 facilitates extraction from oil seeds
-
Triton X-100 stabilizes
-
unstable during purification
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation by formic acid
-
486918
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 90% loss of activity within 1 year
-
-20C, at least 1 month
-
-20C, complete loss of activity in the presence of EDTA and 2-mercaptoethanol
-
-20C, several months
-
-20C, t1/2: 1 month
-
-70 to -20C, 90% loss of activity within 7 days
-
-70C, at least 1 month
-
-80C, several weeks in the presence of 20% v/v glycerol, 0.1% Triton X-100 and dithiothreitol
-
0C, unstable in crude extracts lacking glycerol. Enzyme from fresh extract synthesizes prominent amounts of C14 and C16 acyl chains. After storage at -20C for one or several weeks, enzyme synthesizes predominantly C8 acyl chains
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 proteins alpha2, alpha,beta and beta2
-
immobilized metal ion affinity chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
immobilized metal ion affinity chromatography (Ni2+), anion-exchange chromatography
-
isolation of hexanoyl-enzyme intermediate complex
-
native enzyme from kernel microsomes, solubilization and separation from KAS II by treatment with Triton X-100 and anion exchange chromatography
-
native fatty acid synthase from liver in several steps including gel filtration as the last step
-
partial
recombinant enzyme
recombinant from E. coli as His-tagged protein
-
recombinant from E. coli as His-tagged protein; wild-type and mutants
-
recombinant His-tagged enzyme from Escherichia coli strains XL-1 blue and M15
recombinant His-tagged protein from E. coli
-
recombinant His-tagged protein from E. coli; recombinant His-tagged protein from E. coli
recombinant His-tagged proteins FabH1 and FabH2 from E. coli
-
recombinant His-tagged seed-specific isoform from E. coli
-
recombinant His-tagged synthase III from E. coli
recombinant His-tagged synthase IV from E. coli
-
recombinant soluble NusA-fusion protein FabBF from Escherichia coli strain BL21(DE3) by and gel filtration
-
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
-
synthase I
-
synthase I; synthases II
-
synthase II, recombinant from E. coli
-
synthase III, native wild-type and recombinant from E. coli E103S
-
synthase III-like polyketid synthase recombinant from Streptomyces lividans
-
synthases I and II
synthases II
-