Information on EC 2.3.1.38 - [acyl-carrier-protein] S-acetyltransferase

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

EC NUMBER
COMMENTARY hide
2.3.1.38
-
RECOMMENDED NAME
GeneOntology No.
[acyl-carrier-protein] S-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fatty acid biosynthesis initiation II
-
-
lipid metabolism
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superpathway of fatty acid biosynthesis initiation (E. coli)
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:[acyl-carrier protein] S-acetyltransferase
This enzyme, along with EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. The substrate acetyl-CoA protects the enzyme against inhibition by N-ethylmaleimide or iodoacetamide [4]. This is one of the activities associated with beta-ketoacyl-ACP synthase III (EC 2.3.1.180) [5].
CAS REGISTRY NUMBER
COMMENTARY hide
37257-16-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
safflower
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain E26
-
-
Manually annotated by BRENDA team
Z
-
-
Manually annotated by BRENDA team
Persea sp.
avocado
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene fadA
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + pantetheine
CoA + acetyl-S-pantetheine
show the reaction diagram
acetyl-CoA + [acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
butyryl-CoA + [acyl-carrier protein]
CoA + butyryl-[acyl-carrier protein]
show the reaction diagram
hexanoyl-CoA + [acyl-carrier protein]
CoA + hexanoyl-[acyl-carrier protein]
show the reaction diagram
octanoyl-CoA + [acyl-carrier protein]
CoA + octanoyl-[acyl-carrier protein]
show the reaction diagram
propionyl-CoA + [acyl-carrier protein]
CoA + propionyl-[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
acetyl-CoA + [acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
high ionic strength required for maximal activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
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at high concentration
acyl-carrier protein
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at high concentration
cerulenin
Persea sp.
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antibiotic, weak inhibition
CoA
-
competitive
iodoacetamide
methyl methanethiosulfonate
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weak
N-ethylmaleimide
p-chloromercuribenzoate
-
strong inhibition
p-Substituted mercuribenzoate
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-
pantetheine
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weak, competitive
thiolactomycin
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.05
acetyl-CoA
0.035
acyl-carrier protein
-
-
0.0083
Butyryl-CoA
-
-
0.0086
Hexanoyl-CoA
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0225 - 4.2
acetyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
CoA
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-
3.2
pantetheine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000005
-
-
0.000009
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crude enzyme extract
0.000064
-
-
0.00019
-
-
0.00023
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crude extract
0.0056
0.022
-
purified native wild-type enzyme
0.03
-
partially purified enzyme
0.3
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purified enzyme
0.8
-
approx., purified enzyme
2.68
-
recombinant purified wild-type enzyme
3.22
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recombinant purified wild-type enzyme, carboxyterminally FLAG-tagged
3.81
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recombinant purified wild-type enzyme, carboxyterminally His-tagged
4.53
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recombinant purified mutant R606K
17.8
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recombinant purified mutant R606A
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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assay at
7
Persea sp.
-
-
8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
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about 60% of maximal activity at pH 5.0 and pH 8.5
6.2 - 7.5
Persea sp.
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about half-maximal activity at pH 6.0 and pH 7.5
7.5 - 9.1
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about half-maximal activity at pH 7.5 and about 75% of maximal activity at pH 9.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Persea sp.
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
fatty acid synthase II
Manually annotated by BRENDA team
Persea sp.
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18500
Persea sp.
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gel filtration
48000
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gel filtration
60000
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gel filtration
61000
-
gel filtration
147000
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gel filtration
185000
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gel filtration
additional information
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amino acid sequence, comparison
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 29000, SDS-PAGE
tetramer
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4 * 45000, SDS-PAGE
additional information
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vertebrates, yeast and Mycobacteria fatty acid synthetases contain all individual activities on one or two multifunctional polypeptide chains, plant, Escherichia coli and other prokaryotic fatty acid synthases are non-associated systems of individual enzymes
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
30% loss of activity after 40 min
50
-
t1/2: 18 min
60
-
t1/2: 9 min
100
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inactivation after 1 min
additional information
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
EDTA at 5 mM stabilize
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, unpredictable instability on storage, sometimes total loss of activity occured immediately after thawing
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-20C, at least 1 month
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-20C, less than 10% of activity retained after 1 year
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-20C, several months
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-70C, several months
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0C, inactivation within several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native wild-type and recombinant wild-type and mutant from E. coli
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partial
recombinant mutants from E. coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and sequencing of fadA gene, expression in Escherichia coli of wild-type and C92S mutant
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expression in Escherichia coli
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expression of wild-type and His-tagged mutant S581A as His-tagged proteins in Escherichia coli and as FLAG-tagged proteins in Sf9 insect cells via baculovirus infection
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expression of wild-type and mutants in Escherichia coli BL21 (DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C159A
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no activity
C59S
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no activity
R606A
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oligonucleotide-directed in vitro mutagenesis, 6.6fold increase in activity about 16000fold increase in selectivity for acetyl-CoA against malonyl-CoA, increased production of medium-chain length fatty acids
R606K
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oligonucleotide-directed in vitro mutagenesis, 1.7fold increase in activity about 16fold increase in selectivity for acetyl-CoA against malonyl-CoA
S581A
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nearly no remaining activity, below 0.03% compared to wild-type
C92S
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no remaining activity acetyl-CoA:acyl carrier protein transacylase activity, but remaining strongly reduced thiolase activity
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme purified from E. coli, refolding after treatment of inclusion bodies with urea
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