Information on EC 2.3.1.41 - beta-ketoacyl-[acyl-carrier-protein] synthase I and Organism(s) Homo sapiens

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


The taxonomic range for the selected organisms is: Homo sapiens

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
structure-activity analysis, reaction mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5Z)-dodecenoate biosynthesis I
-
-
(5Z)-dodecenoate biosynthesis II
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8-amino-7-oxononanoate biosynthesis I
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fatty acid biosynthesis initiation II
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fatty acid biosynthesis initiation III
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fatty acid elongation -- saturated
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-
gondoate biosynthesis (anaerobic)
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mycolate biosynthesis
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octanoyl-[acyl-carrier protein] biosynthesis (mitochondria, yeast)
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-
oleate biosynthesis IV (anaerobic)
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palmitate biosynthesis I (animals and fungi)
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palmitate biosynthesis II (bacteria and plants)
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palmitoleate biosynthesis I (from (5Z)-dodec-5-enoate)
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stearate biosynthesis II (bacteria and plants)
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stearate biosynthesis III (fungi)
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superpathway of fatty acid biosynthesis initiation (E. coli)
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superpathway of mycolate biosynthesis
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arachidonate biosynthesis
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lipid metabolism
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palmitate biosynthesis
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Fatty acid biosynthesis
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Biotin metabolism
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Metabolic pathways
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxobutanoyl-[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
-
-
-
-
?
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
-
-
-
-
?
hexanoyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
3-oxooctanoyl-[acyl-carrier protein] + 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
-
-
-
-
?
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-[acyl-carrier protein]
3-oxooctanoyl-[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
additional information
?
-
-
important role in generation of the lipoic acid precursor octanoyl-acyl-carrier protein
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-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cerulenin
additional information
inhibitor binding structure determination
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
acetyl-[acyl-carrier protein]
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pH 6.8, 37°C
0.0039
butanoyl-[acyl-carrier protein]
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pH 6.8, 37°C
0.0018
decanoyl-[acyl-carrier protein]
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pH 6.8, 37°C
0.0095
dodecanoyl-[acyl-carrier protein]
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pH 6.8, 37°C
0.0019
hexanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0508
myristoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
0.0109
octanoyl-[acyl-carrier protein]
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pH 6.8, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91.2
butanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
551
decanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
303
dodecanoyl-[acyl-carrier protein]
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pH 6.8, 37°C
353
hexanoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
6
myristoyl-[acyl-carrier protein]
-
pH 6.8, 37°C
66
octanoyl-[acyl-carrier protein]
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pH 6.8, 37°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low level
Manually annotated by BRENDA team
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most abundant
Manually annotated by BRENDA team
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low level
Manually annotated by BRENDA team
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low level
Manually annotated by BRENDA team
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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
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45800
-
x * 45800, SDS-PAGE, recombinant protein without N-terminal targeting sequence, with His-tag
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45800, SDS-PAGE, recombinant protein without N-terminal targeting sequence, with His-tag
dimer
secondary structure, a dimer with an alpha-beta-alpha-beta-alpha-thiolase fold capped by an alpha-helical region connecting the strands of the N-terminal beta-sheet, crystal structure analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
mitochondrial targeting sequence of 38 residues
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strains XL-1 blue and M15
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of the His-tagged enzyme in Escherichia coli strains XL-1 blue and M15
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a target for antibacterial drugs