Information on EC 2.3.1.86 - fatty-acyl-CoA synthase

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

EC NUMBER
COMMENTARY hide
2.3.1.86
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RECOMMENDED NAME
GeneOntology No.
fatty-acyl-CoA synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
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decarboxylation
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-
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redox reaction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(5Z)-dodec-5-enoate biosynthesis
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Fatty acid biosynthesis
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fatty acid biosynthesis (plant mitochondria)
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fatty acid biosynthesis initiation 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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fatty acids biosynthesis (yeast)
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Metabolic pathways
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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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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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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:malonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing)
The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, 3-oxoacyl-[acyl-carrier-protein] synthase, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid ester dehydrogenase. The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid.
CAS REGISTRY NUMBER
COMMENTARY hide
9045-77-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
type II fatty acid synthase complex, expression in Sf9 cells
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Manually annotated by BRENDA team
fatty acid synthase alpha-subunit
SwissProt
Manually annotated by BRENDA team
strain SS9
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Manually annotated by BRENDA team
strain SS9
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Manually annotated by BRENDA team
pea
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Manually annotated by BRENDA team
strain Fleishmann, wild type and protease-negative pep4-mutant
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Manually annotated by BRENDA team
strain X-2180-A
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Manually annotated by BRENDA team
spinach
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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construction of Fas2 disruptants influences virulence, unability to form normal biofilms
physiological function
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essential for growth in absence of exogenous fatty acids, involved in unsatured fatty acid production
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 + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
show the reaction diagram
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
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 + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-phosphopantetheine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-Dibromo-2-propanone
5,5'-dithio-bis(2-nitrobenzoic acid)
cerulenin
iodoacetamide
methylamine tungstad
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inactivation within 24 h
N-ethylmaleimide
p-chloromercuribenzoate
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complete inhibition of type II fatty acid synthase at 1 mM
thiolactomycin
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antibiotic and it's analogues, 50% inhibition of the overall activity at 0.17 mM, effect of antibiotic on compounds of the enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-O-methylmannose
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0.1 mM, lowers Km 4fold, activation by relieving product inhibition by binding long-chain acyl-CoA
6-O-methylglucose
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0.1 mM, lowers Km 4fold, activation by relieving product inhibition by binding long-chain acyl-CoA
ATP
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stimulatory at suboptimal but not at saturating substrate concentrations
cysteine
glutathione
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activation
Triton X-100
additional information
-
no activation by DTT
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 0.8
acetyl-CoA
0.83
decanoyl-CoA
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0.05
Lauroyl-CoA
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0.0096 - 0.04
malonyl-CoA
0.4
myristoyl-CoA
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0.33
Octanoyl-CoA
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0.13
palmitoyl-CoA
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-
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.062
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substrates: acetoacetyl-cysteamine, malonyl-CoA and NADPH
0.8 - 0.83
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malonyl-CoA
1.25 - 1.75
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substrate: C2-unit
1.6
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substrates: acetoacetyl-CoA, malonyl-CoA and NADPH H
2.5 - 3.5
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NADPH
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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beta-ketoacyl synthetase activity, assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
324900
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calculated from nucleotide sequence
1390000
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sedimentation velocity data
2300000
2370000
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sedimentation equilibrium method
2400000
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sedimentation velocity
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 46000, SDS-PAGE, x * 43000, calculated
dodecamer
hexamer
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homohexamer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of yeast FAS reveals that this large, macromolecular assembly functions as a six-chambered reactor for fatty acid synthesis. Each of the six chambers functions independently and has in its chamber wall all of the catalytic units required for fatty acid priming, elongation, and termination, while one substrate-shuttling component, ACP, is located inside each chamber and functions like a swinging arm. Surprisingly, however, the step at which the reactor is activated must occur before the complete assembly of the particle since the PPT domain that attaches the pantetheine arm to ACP lies outside the assembly, inaccessible to ACP that lies inside. Remarkably, the architectural complexity of the FAS particle results in the simplicity of the reaction mechanisms for fatty acid synthesis
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structure determined at 3.1 A resolution with its acyl carrier protein stalled at the active site of ketoacyl synthase. The structure shows the direct interaction of acyl carrier protein with one of the key catalytic centers in a multifunctional enzyme and suggest a model for substrate delivery that might apply to the other catalytic domains as well; structure of the Saccharomyces cerevisiae FAS determined at 3.1 A resolution with its acyl carrier protein stalled at the active site of ketoacyl synthase. The structure of the yeast FAS complex shows the direct interaction of acyl carrier protein with one of the key catalytic centers in a multifunctional enzyme and suggests a model for substrate delivery
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5 A resolution
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crystal structure at 3.1 A resolution
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol, inactivation during storage
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acylation of free protein amino groups leads to reversible dissociation into subunits
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low ionic strength leads to inactivation
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low ionic strength, 0.005 M, leads to dissociation into subunits, partially reactivated by increasing the ionic strength to 0.5 M
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PMSF ensures isolation of native enzyme
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
under 100 atm nitrogen, at 4C 1-20 h stable, 40% loss of activity after 40 h
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487604
under 100 atm oxygen, at 4C 1-2 h stable, 48% and 90% loss of activity after 20 h and 40 h, respectively, DTT does not restore activity
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487604
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable in 90% ammonium sulfate solution containing 0.1 M potassium phosphate, pH 6.5, and 1 mM DTT
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4C, precipitate in 50% ammonium sulfate solution, several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homogeneity
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isolation and sequencing of active-site peptides with transacylase activity
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isolation of alpha- and beta-subunits by acylation
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isolation of alpha- and beta-subunits; isolation of alpha- and beta-subunits by citraconic and dimethylmaleic anhydride modification
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isolation of alpha- and beta-subunits; isolation of alpha- and beta-subunits by citraconic and dimethylmaleic anhydride modification or as 3,4,5,6-tetrahydrophthalate derivatives
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isolation of peptides after proteolysis
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partial purification of components
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purification of 2 structurally related but functionally differentiated fatty acid synthases: FAS-A and FAS-B, homogeneity
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purification of acyl carrier protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
transformation technique, plasmid YEpFAS2 transformed to and expressed in Escherichia coli maxi-cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1305A
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peripheral SH-group defective
S180G
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central SH-group defective
S5421Q
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malonyl/palmitoyl transferase defective
S819Q
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acyltransferase defective
T181G
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central SH-group defective
A45C
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about 5% reduction in overall enzyme activity
A45G
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about 15% reduction in overall enzyme activity
A45W
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about 10% reduction in overall enzyme activity
E41D
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about 10% reduction in overall enzyme activity
E41K
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no residual activity
V43I
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no reduction in overall enzyme activity
additional information
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FAS2 KO cells, construction of Fas2 disruptants influences virulence, unability to form normal biofilms
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis under mild acidic condition leads to unmodified subunits, which can be reconstituted to form a complex displaying about 60% of the original activity
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low concentration of phosphate buffer causes dissociation into inactive species, reaggregation and reactivation can be partially achieved by dialysis against 0.5 M phosphate buffer
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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potential treatment of infection of humans with Candida parapsilosis
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