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
2.3.1.86
-
RECOMMENDED NAME
GeneOntology No.
fatty-acyl-CoA synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 mechanism
-
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
show the reaction diagram
reaction mechanism; structure; structure and regulation
-
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
show the reaction diagram
reaction mechanism
-
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
show the reaction diagram
reaction mechanism; structure
-
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
show the reaction diagram
structure
-
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+
show the reaction diagram
structure
Saccharomyces cerevisiae Fleishmann
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
decarboxylation
-
-
-
-
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
cis-dodecenoyl biosynthesis
-
Fatty acid biosynthesis
-
fatty acid biosynthesis (plant mitochondria)
-
fatty acid biosynthesis initiation I
-
fatty acid biosynthesis initiation II
-
fatty acid biosynthesis initiation III
-
fatty acid elongation -- saturated
-
fatty acids biosynthesis (yeast)
-
Metabolic pathways
-
octanoyl-ACP biosynthesis (mitochondria, yeast)
-
palmitate biosynthesis I (animals and fungi)
-
palmitate biosynthesis II (bacteria and plants)
-
stearate biosynthesis II (bacteria and plants)
-
stearate biosynthesis III (fungi)
-
superpathway of fatty acid biosynthesis initiation (E. coli)
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
fatty acid synthase
-
-
yeast fatty acid synthase
-
-
-
-
yeast fatty acid synthase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9045-77-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
var. bacillaris
-
-
Manually annotated by BRENDA team
type II fatty acid synthase complex, expression in Sf9 cells
-
-
Manually annotated by BRENDA team
fatty acid synthase alpha-subunit
SwissProt
Manually annotated by BRENDA team
brewer's yeast
-
-
Manually annotated by BRENDA team
mutants lacking endogenous de novo fatty acid synthesis
-
-
Manually annotated by BRENDA team
strain Fleishmann, wild type and protease-negative pep4-mutant
-
-
Manually annotated by BRENDA team
strain X-2180-A; wild-type haploid strain X2180-1A and 52 fas-mutant strains
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae Fleishmann
strain Fleishmann, wild type and protease-negative pep4-mutant
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae X-2180-A
strain X-2180-A
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
construction of Fas2 disruptants influences virulence, unability to form normal biofilms
physiological function
-
essential for growth in absence of exogenous fatty acids, involved in unsatured fatty acid production
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 + 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 + 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 + 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
-
-
FAS-A mainly synthesizes the C18 fatty acids oleate and stearate with only traces of palmitate, the major product of FAS-B is pamitate
?
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
-
-
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
show the reaction diagram
-
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
-
-
?
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
-
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
?
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
-
mutants require acyl-CoA primers of 10 or more carbon atoms, maximal activity with 12-14 carbon atoms
-
-
?
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
-
primers instead of acetyl-CoA: propionyl-CoA, butyryl-CoA or hexanoyl-CoA
-
-
-
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
-
intermediates are never released into the medium
-
-
?
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
Saccharomyces cerevisiae X2180-1A
-
mutants require acyl-CoA primers of 10 or more carbon atoms, maximal activity with 12-14 carbon atoms
-
-
?
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
Saccharomyces cerevisiae X-2180-A
-
-
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
Saccharomyces cerevisiae Fleishmann
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
Saccharomyces cerevisiae X-2180-A
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
Saccharomyces cerevisiae Fleishmann
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
acetyl-CoA + malonyl-CoA + NADH + NADPH
?
show the reaction diagram
Saccharomyces cerevisiae X-2180-A
-
multifunctional enzyme involved in yeast fat metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4'-phosphopantetheine
-
4.0-5.0 mol per mol enzyme; 4.0-5.0 mol per mol enzyme or about 1 mol per 2 subunits; alpha-subunit bears prosthetic group
4'-phosphopantetheine
-
requirement, pantetheinate-free mutants have no beta-ketoacyl synthetase activity
4'-phosphopantetheine
-
4.0-5.0 mol per mol enzyme or about 1 mol per 2 subunits
FMN
-
requirement, enoyl reductase activity, associated with beta-subunit, 6 mol per mol synthetase
FMN
-
4 mol FMN per mol of enzyme complex
NADH
-
requirement, 25% as efficient as NADPH
NADPH
-
requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,3-Dibromo-2-propanone
-
-
1,3-Dibromo-2-propanone
-
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)
-
covalent binding to palmitoyl residues, malonyl-CoA protects
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
cerulenin
-
complete inhibition of type II fatty acid synthase at 0.1 mM
iodoacetamide
-
complete inhibition of type II fatty acid synthase at 1 mM
iodoacetamide
-
beta-ketoacyl synthetase; no inhibition of acetyl transferase activity
iodoacetamide
-
no inhibition of acetyl transferase activity; pH-independent between 5.0 and 9.0
iodoacetamide
-
irreversible
Methylamine tungstad
-
inactivation within 24 h
N-ethylmaleimide
-
complete inhibition of type II fatty acid synthase at 1 mM
N-ethylmaleimide
-
no inhibition of acetyl transferase activity
N-ethylmaleimide
-
no inhibition of acetyl transferase activity; pH-dependent
p-chloromercuribenzoate
-
complete inhibition of type II fatty acid synthase at 1 mM
thiolactomycin
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-O-methylmannose
-
0.1 mM, lowers Km 4fold, activation by relieving product inhibition by binding long-chain acyl-CoA
6-O-methylglucose
-
0.1 mM, lowers Km 4fold, activation by relieving product inhibition by binding long-chain acyl-CoA
ATP
-
stimulatory at suboptimal but not at saturating substrate concentrations
cysteine
-
activation
Triton X-100
-
leads to increasing turnover rate of acyl-CoA
glutathione
-
activation
additional information
-
no activation by DTT
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.09
-
acetyl-CoA
-
in presence of polysaccharide
0.8
-
acetyl-CoA
-
-
0.83
-
Decanoyl-CoA
-
-
0.05
-
Lauroyl-CoA
-
-
0.0096
-
malonyl-CoA
-
in presence of polysaccharide
0.4
-
myristoyl-CoA
-
-
0.33
-
Octanoyl-CoA
-
-
0.13
-
palmitoyl-CoA
-
-
0.04
-
malonyl-CoA
-
-
additional information
-
additional information
-
specific activities for acetyl-CoA derivatives
-
additional information
-
additional information
-
kinetics of transacylase activity
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.062
-
-
substrates: acetoacetyl-cysteamine, malonyl-CoA and NADPH
0.8
0.83
-
malonyl-CoA
1.25
1.75
-
substrate: C2-unit
1.6
-
-
substrates: acetoacetyl-CoA, malonyl-CoA and NADPH H
additional information
-
-
data of partial reactions of fatty acid synthetase, different fas-mutants of Saccharomyces cerevisiae
additional information
-
-
comparison of partial activities of alpha- and beta-subunits with that of the native complex
additional information
-
-
specific activities of components
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
beta-ketoacyl synthetase activity, assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
324900
-
-
calculated from nucleotide sequence
1390000
-
-
sedimentation velocity data
2300000
-
-
analytical ultracentrifugation
2300000
-
-
sedimentation equilibrium
2370000
-
-
sedimentation equilibrium method
2400000
-
-
sedimentation velocity
additional information
-
-
MW of components
additional information
-
-
-
additional information
-
-
alpha6beta6-complex of multifunctional subunits; amino acid sequence of acyl-carrier-protein
additional information
-
-
MW of components
additional information
-
-
amino acid composition
additional information
-
-
alpha6beta6-complex of multifunctional subunits
additional information
-
-
amino acid composition
additional information
-
-
alpha6beta6-complex of multifunctional subunits; amino acid composition
additional information
-
-
MW of components
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 46000, SDS-PAGE, x * 43000, calculated
dodecamer
-
alpha6,beta6, 6 * 185000 + 6 * 180000, SDS-PAGE; alpha6,beta6, 6 * 213000 + 6 * 203000, Tris-glycine-SDS-PAGE
dodecamer
-
alpha6,beta6, 6 * 213000 + 6 * 203000, Tris-glycine-SDS-PAGE
dodecamer
-
active enzyme centrifugation; alpha6,beta6, 6 * 213000 + 6 * 203000, Tris-glycine-SDS-PAGE
dodecamer
Saccharomyces cerevisiae Fleishmann
-
active enzyme centrifugation; alpha6,beta6, 6 * 213000 + 6 * 203000, Tris-glycine-SDS-PAGE
-
hexamer
-
homohexamer
additional information
-
fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and Escherichia coli consist of non-associated individual enzymes
additional information
-
-
additional information
-
fatty acid synthetases of vertebrates and yeast are stable enzyme complexes of multifunctional polypeptide chains, the fatty acid synthetases of plants and Escherichia coli consist of non-associated individual enzymes
additional information
-
two de novo fatty acid synthases, a true multienzyme complex in the cytosol and a plastid-localized type II fatty acid synthase composed of discrete enzymes and acyl carrier protein
additional information
-
identical subunits, SDS-PAGE
additional information
-
multifunctional subunits
additional information
Saccharomyces cerevisiae Fleishmann
-
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
5 A resolution
-
crystal structure at 3.1 A resolution
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
low ionic strength, 0.005 M, leads to dissociation into subunits, partially reactivated by increasing the ionic strength to 0.5 M
-
2-mercaptoethanol, inactivation during storage
-
acylation of free protein amino groups leads to reversible dissociation into subunits
-
low ionic strength leads to inactivation
-
PMSF ensures isolation of native enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
under 100 atm nitrogen, at 4C 1-20 h stable, 40% loss of activity after 40 h
-
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
-
487604
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, stable in 90% ammonium sulfate solution containing 0.1 M potassium phosphate, pH 6.5, and 1 mM DTT
-
4C, precipitate in 50% ammonium sulfate solution, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification of 2 structurally related but functionally differentiated fatty acid synthases: FAS-A and FAS-B, homogeneity
-
purification of acyl carrier protein
-
partial purification of components
-
homogeneity
-
isolation and sequencing of active-site peptides with transacylase activity
-
isolation of alpha- and beta-subunits by acylation
-
isolation of alpha- and beta-subunits; isolation of alpha- and beta-subunits by citraconic and dimethylmaleic anhydride modification
-
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
-
isolation of peptides after proteolysis
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transformation technique, plasmid YEpFAS2 transformed to and expressed in Escherichia coli maxi-cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C1305A
-
peripheral SH-group defective
S180G
-
central SH-group defective
S5421Q
-
malonyl/palmitoyl transferase defective
S819Q
-
acyltransferase defective
T181G
-
central SH-group defective
A45C
-
about 5% reduction in overall enzyme activity
A45G
-
about 15% reduction in overall enzyme activity
A45W
-
about 10% reduction in overall enzyme activity
E41D
-
about 10% reduction in overall enzyme activity
E41K
-
no residual activity
V43I
-
no reduction in overall enzyme activity
additional information
-
FAS2 KO cells, construction of Fas2 disruptants influences virulence, unability to form normal biofilms
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
hydrolysis under mild acidic condition leads to unmodified subunits, which can be reconstituted to form a complex displaying about 60% of the original activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
potential treatment of infection of humans with Candida parapsilosis