BRENDA - Enzyme Database
show all sequences of 2.3.1.221

Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization

Crawford, J.M.; Korman, T.P.; Labonte, J.W.; Vagstad, A.L.; Hill, E.A.; Kamari-Bidkorpeh, O.; Tsai, S.C.; Townsend, C.A.; Nature 461, 1139-1143 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant proteins in Escherichia coli strains BL21(DE3) or Rosetta2(DE3)
Aspergillus parasiticus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
Aspergillus parasiticus
-
7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus parasiticus
-
gene pksA
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant proteins from Escherichia coli strains BL21(DE3) or Rosetta2(DE3)
Aspergillus parasiticus
Reaction
Reaction
Commentary
Organism
7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
reaction mechanism, overview. The SAT domain in PksA selects a hexanoyl starter unit. The MAT domain loads the free ACP with malonyl units. After seven successive condensation events with malonyl-ACP catalysed in te ketoacyl synthase domain, the linear ACP-bound polyketide is cyclized (C4-C9 and C2-C11 cyclization events) and aromatized in the product template domain to give the bicyclic intermediate. The thioesterase domain catalyses C-C cyclization to release anthrone, which undergoes oxidation to the anthraquinone norsolorinic acid, to initiate the complex biosynthetic pathway to aflatoxin B1
Aspergillus parasiticus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
-
723262
Aspergillus parasiticus
7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
domain organization of PksA with acyl-carrier protein (ACP), acyl transacylase (AT), dehydrase (DH), enoyl reductase (ER), ketoreductase (KR), ketoacyl synthase (KS), pseudomethyltransferase (PsiMT), starter unit:ACP transacylase (SAT), and thioesterase (TE), structure model, overview
Aspergillus parasiticus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant proteins in Escherichia coli strains BL21(DE3) or Rosetta2(DE3)
Aspergillus parasiticus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
Aspergillus parasiticus
-
7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant proteins from Escherichia coli strains BL21(DE3) or Rosetta2(DE3)
Aspergillus parasiticus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
-
723262
Aspergillus parasiticus
7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
domain organization of PksA with acyl-carrier protein (ACP), acyl transacylase (AT), dehydrase (DH), enoyl reductase (ER), ketoreductase (KR), ketoacyl synthase (KS), pseudomethyltransferase (PsiMT), starter unit:ACP transacylase (SAT), and thioesterase (TE), structure model, overview
Aspergillus parasiticus
General Information
General Information
Commentary
Organism
metabolism
biosynthesis of norsolorinic acid anthrone by PksA, detailed overview
Aspergillus parasiticus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
biosynthesis of norsolorinic acid anthrone by PksA, detailed overview
Aspergillus parasiticus
Other publictions for EC 2.3.1.221
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
722459
Vagstad
Interrogation of global active ...
Aspergillus parasiticus
J. Am. Chem. Soc.
134
6865-6877
2012
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723638
Korman
Structure and function of an i ...
Aspergillus sp.
Proc. Natl. Acad. Sci. USA
107
6246-6251
2010
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1
4
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4
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1
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2
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723262
Crawford
Structural basis for biosynthe ...
Aspergillus parasiticus
Nature
461
1139-1143
2009
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1
1
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721052
Crawford
Deconstruction of iterative mu ...
Aspergillus parasiticus
Science
320
243-246
2008
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1
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2
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723194
Chang
The Aspergillus parasiticus po ...
Aspergillus parasiticus, Aspergillus parasiticus SRRC 2043 / RHN1
Mol. Gen. Genet.
248
270-277
1995
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