Information on EC 2.3.1.221 - noranthrone synthase

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The expected taxonomic range for this enzyme is: Aspergillus

EC NUMBER
COMMENTARY hide
2.3.1.221
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RECOMMENDED NAME
GeneOntology No.
noranthrone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(1'S,5'S)-averufin biosynthesis
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Aflatoxin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:hexanoate malonyltransferase (norsolorinic acid anthrone-forming)
A multi-domain polyketide synthase involved in the synthesis of aflatoxins in the fungus Aspergillus parasiticus. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pksA
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
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PksA, which initiates biosynthesis of the environmental carcinogen aflatoxin B1, is one of the multidomain iterative polyketide synthases, IPKSs
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7 malonyl-CoA + acetyl-[acyl-carrier protein]
?
show the reaction diagram
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-
-
-
?
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
show the reaction diagram
additional information
?
-
-
processivity of polyketide extension and substrate specificity, overview. The enzyme shows activity against hexanoyl- and acetyl-, but not malonyl-CoA. Rapid loading of extension units onto the carrier domain facilitates efficient chain extension in a manner kinetically favorable to ultimate product formation. Essential roles of the product template and thioesterase domains for cyclization and product release, editing role for the thioesterase domain
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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
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.38
acetyl-[acyl-carrier protein]
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pH 7.0, 22°C
1.46
hexanoyl-[acyl-carrier protein]
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pH 7.0, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0407
acetyl-[acyl-carrier protein]
Aspergillus parasiticus
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pH 7.0, 22°C
0.0472
hexanoyl-[acyl-carrier protein]
Aspergillus parasiticus
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pH 7.0, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026
acetyl-[acyl-carrier protein]
Aspergillus parasiticus
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pH 7.0, 22°C
3373
0.032
hexanoyl-[acyl-carrier protein]
Aspergillus parasiticus
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pH 7.0, 22°C
4018
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant selenomethionine-labeled of PksA TE, sitting drop vapour diffusion method, 5 mg/ml protein in 20 mM Tris-HCl pH 7.5 containing 5% glycerol and 2 mM DTT is mixed with well solution containing 0.2 M ammonium acetate, 0.1 M sodium citrate pH 5.6, and 30% PEG 4000, 25°C, 2 days, X-ray diffraction structure determination and analysis, modeling
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C- or N-terminally His6-tagged mono-, di-, and tridomains protein fragments from Escherichia coli by metal affinity cromatography
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recombinant His-tagged thioesterase/Claisen cyclase and selenomethionine-labeled PksA TE from Escherichia coli
recombinant N-terminally His6-tagged enzyme domains from Escherichia coli strain BL21(DE3)
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recombinant wild-type and mutant proteins from Escherichia coli strains BL21(DE3) or Rosetta2(DE3)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His6-tagged enzyme domains in Escherichia coli strain BL21(DE3)
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expression of recombinant His-tagged thioesterase/Claisen cyclase in Escherichia coli, expression of the selenomethionine-labeled PksA TE in Escherichia coli methionine auxotroph strain B834(DE3)
expression of wild-type and mutant proteins in Escherichia coli strains BL21(DE3) or Rosetta2(DE3)
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gene pksA, cloning of various mono-, di-, and tridomains for combinatorial reconstitution experiments, expression of the either C- or N-terminally His6-tagged protein fragments in Escherichia coli
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gene pksA, DNA and amino acid sequence determination and analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S1937A
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inactive mutant
D1964N
site-directed mutagenesis of a catalytic residue
D2070N
site-directed mutagenesis, the mutation results in only a slightly reduced rate of hydrolysis compared to the apo-mutant
H2088F
site-directed mutagenesis of a catalytic residue
S1937A
site-directed mutagenesis of a catalytic residue
additional information