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Information on EC 2.3.1.86 - fatty-acyl-CoA synthase system
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EC Tree
2.3.1.86 fatty-acyl-CoA synthase systemIUBMB Comments
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, beta-ketoacyl-[acyl-carrier-protein] synthase I, 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-hydroxyacyl-[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 system differs from the animal system (EC 2.3.1.85, fatty-acid synthase system) 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.
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Word Map
- 2.3.1.86
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udp-glucuronosyltransferase
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glucuronidation
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farnesoid
- carvedilol
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extrahepatic
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acid-conjugating
- parapsilosis
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hyodeoxycholic
- 4-hydroxyestrone
- analysis
- medicine
- biofuel production
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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7
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14
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14
=
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7
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7
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14
+
7
Synonyms
cpfas2, fatty-acyl-coa synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FAS1
fas2
fatty-acyl-CoA synthase
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yeast fatty acid synthase
yeast fatty acid synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
reaction mechanism
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acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
reaction mechanism
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acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
structure
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acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
structure and regulation
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acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
structure
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acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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decarboxylation
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redox reaction
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PATHWAY SOURCE
PATHWAYS
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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, beta-ketoacyl-[acyl-carrier-protein] synthase I, 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-hydroxyacyl-[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 system differs from the animal system (EC 2.3.1.85, fatty-acid synthase system) 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.
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CAS REGISTRY NUMBER
COMMENTARY
9045-77-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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FAS-A mainly synthesizes the C18 fatty acids oleate and stearate with only traces of palmitate, the major product of FAS-B is pamitate
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acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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synthesis of saturated and unsaturated fatty acids, FAS-B cannot synthesize oleic acid
?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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primers instead of acetyl-CoA: propionyl-CoA, butyryl-CoA or hexanoyl-CoA
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?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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-
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?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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-
-
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?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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stable multifunctional enzyme complex: carries acetyl-CoA and malonyl-CoA transacylase, beta-ketoacyl reductase, beta-hydroxyacyl dehydrase activities on beta-subunits and condensing enzyme, i.e. beta-ketoacyl synthetase, enoylacyl reductase activities and acyl-carrier-protein components on alpha-subunits
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acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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S-acetylpantetheine and S-malonylpantetheine and saturated acetyl-CoA derivatives can replace acetyl-CoA and malonyl-CoA
palmitoyl-CoA and steraoyl-CoA are main products, myristoyl-CoA is produced in small amounts
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acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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mutants require acyl-CoA primers of 10 or more carbon atoms, maximal activity with 12-14 carbon atoms
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acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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intermediates are never released into the medium
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acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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mutants require acyl-CoA primers of 10 or more carbon atoms, maximal activity with 12-14 carbon atoms
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?
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+
palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
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acetyl-CoA + malonyl-CoA + NADH + NADPH
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multifunctional enzyme involved in yeast fat metabolism
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acetyl-CoA + malonyl-CoA + NADH + NADPH
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multifunctional enzyme involved in yeast fat metabolism
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acetyl-CoA + malonyl-CoA + NADH + NADPH
?
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multifunctional enzyme involved in yeast fat metabolism
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acetyl-CoA + malonyl-CoA + NADH + NADPH
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multifunctional enzyme involved in yeast fat metabolism
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additional information
?
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fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and E. coli consist of non-associated individual enzymes
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?
additional information
?
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narrow substrate specificity for both the acyl donor and the acyl carrier protein acceptor. Exclusive transfer of malonyl-CoA moieties to the mitochondrial holoacyl carrier protein
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?
additional information
?
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fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and E. coli consist of non-associated individual enzymes
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
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multifunctional enzyme involved in yeast fat metabolism
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?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
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multifunctional enzyme involved in yeast fat metabolism
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-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
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multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
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multifunctional enzyme involved in yeast fat metabolism
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4'-phosphopantetheine
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4.0-5.0 mol per mol enzyme or about 1 mol per 2 subunits
4'-phosphopantetheine
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requirement, pantetheinate-free mutants have no beta-ketoacyl synthetase activity
FMN
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requirement, enoyl reductase activity, associated with beta-subunit, 6 mol per mol synthetase
NADPH
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requirement
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1,3-Dibromo-2-propanone
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complete inhibition at 0.005 mM after 1 min, cross-links alpha-, not beta-subunits, inhibits only beta-ketoacyl synthetase reaction, acetyl-CoA prevents, malonyl-CoA prevents only slightly
5,5'-dithio-bis(2-nitrobenzoic acid)
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covalent binding to palmitoyl residues, malonyl-CoA protects
iodoacetamide
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beta-ketoacyl synthetase; no inhibition of acetyl transferase activity
iodoacetamide
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no inhibition of acetyl transferase activity; pH-independent between 5.0 and 9.0
N-ethylmaleimide
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complete inhibition of type II fatty acid synthase at 1 mM
N-ethylmaleimide
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no inhibition of acetyl transferase activity; pH-dependent
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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specific activities for acetyl-CoA derivatives
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additional information
additional information
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kinetics of transacylase activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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data of partial reactions of fatty acid synthetase, different fas-mutants of Saccharomyces cerevisiae
additional information
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comparison of partial activities of alpha- and beta-subunits with that of the native complex
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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486863, 487574, 487600, 487603, 487604, 487608, 487609, 487610, 487618, 677130, 685985, 748546, 756246, 757575
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brenda
P07149 i.e. subunit FAS1, P19097 i.e. subunit FAS2
UniProt
brenda
P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2
UniProt
brenda
P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2, Q12513 i.e. gamma-subunit Tma17
UniProt
brenda
wild-type haploid strain X2180-1A and 52 fas-mutant strains
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brenda
P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2
UniProt
brenda
P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2, Q12513 i.e. gamma-subunit Tma17
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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cytosol accounts for almost 80% of the total [3H]acetate incorporated into fatty acids by whole cell lysates
brenda
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cytosol accounts for almost 80% of the total [3H]acetate incorporated into fatty acids by whole cell lysates
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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construction of Fas2 disruptants influences virulence, unability to form normal biofilms
metabolism
physiological function
metabolism
cotranslational assembly of yeast FAS. The N-terminus of subunit alpha (FAS2) intertwines with the C-terminus of subunt beta (FAS1) by getting sandwiched between a structured malonyl-palmitoyl-transferase core fold and a alpha67/alpha68 element. The cotranslationally formed interaction is sensitive to perturbations. The assembly of yeast FAS can also proceed when subunit borders are shifted. Linking subunits of FAS at the cotranslationally formed interface and introducing splitting sites at two other sites, within the alpha-helical bundle structure 4-helical bundle of subunit alpha and within the antiparallel 6-stranded beta-sheet of beta, leads to intact protein. The cotranslational assembly may not be strictly sequence- or site-specific
metabolism
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cotranslational assembly of yeast FAS. The N-terminus of subunit alpha (FAS2) intertwines with the C-terminus of subunt beta (FAS1) by getting sandwiched between a structured malonyl-palmitoyl-transferase core fold and a alpha67/alpha68 element. The cotranslationally formed interaction is sensitive to perturbations. The assembly of yeast FAS can also proceed when subunit borders are shifted. Linking subunits of FAS at the cotranslationally formed interface and introducing splitting sites at two other sites, within the alpha-helical bundle structure 4-helical bundle of subunit alpha and within the antiparallel 6-stranded beta-sheet of beta, leads to intact protein. The cotranslational assembly may not be strictly sequence- or site-specific
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physiological function
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essential for growth in absence of exogenous fatty acids, involved in unsatured fatty acid production
physiological function
translation machinery-associated protein Tma17 copurifies with FAS complex. 6 copies of Tma17p can simultaneously bind to one FAS molecule, binding follows a positive cooperativity. Tma17 acts as FAS gamma subunit regulating the activity in response to the abundance of cosubstrate NADPH
physiological function
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translation machinery-associated protein Tma17 copurifies with FAS complex. 6 copies of Tma17p can simultaneously bind to one FAS molecule, binding follows a positive cooperativity. Tma17 acts as FAS gamma subunit regulating the activity in response to the abundance of cosubstrate NADPH
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Show AA Sequence and Transmembrane Helices (1828 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
203000
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alpha6,beta6, 6 * 213000 + 6 * 203000, Tris-glycine-SDS-PAGE
213000
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alpha6,beta6, 6 * 213000 + 6 * 203000, Tris-glycine-SDS-PAGE
2300000
additional information
additional information
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alpha6beta6-complex of multifunctional subunits