2.3.1.221: noranthrone synthase
This is an abbreviated version!
For detailed information about noranthrone synthase, go to the full flat file.
Word Map on EC 2.3.1.221
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2.3.1.221
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sporopollenin
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tetraketide
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exine
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anther
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microspore
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tapetal
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reductase1
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halogenase
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prenyltransferase
- 2.3.1.221
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sporopollenin
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tetraketide
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exine
-
anther
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microspore
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tapetal
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reductase1
- halogenase
- prenyltransferase
Reaction
7 malonyl-CoA + = 7 CoA + + + 7 CO2 + 2 H2O
Synonyms
norsolorinic acid anthrone synthase, norsolorinic acid anthrone-producing polyketide synthase, PksA, polyketide synthase A
ECTree
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General Information
General Information on EC 2.3.1.221 - noranthrone synthase
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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
the pksA gene is located in the aflatoxin pathway gene cluster and is linked to the nor-1 gene, an aflatoxin pathway gene required for converting norsolorinic acid to averantin
evolution
Aspergillus parasiticus SRRC 2043 / RHN1
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the pksA gene is located in the aflatoxin pathway gene cluster and is linked to the nor-1 gene, an aflatoxin pathway gene required for converting norsolorinic acid to averantin
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strain SRRC 2043 is a disruption mutant defective in the pksA locus. Disruption of pksA results in an inability to produce aflatoxin intermediates
malfunction
Aspergillus parasiticus SRRC 2043 / RHN1
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strain SRRC 2043 is a disruption mutant defective in the pksA locus. Disruption of pksA results in an inability to produce aflatoxin intermediates
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biosynthesis of norsolorinic acid anthrone by PksA, detailed overview
metabolism
pksA is a polyketide synthase gene required for the early steps of aflatoxin biosynthesis
metabolism
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PksA is involved in the synthesis of norsolorinic acid, an intermediate in the biosynthesis of the environmental carcinogen aflatoxin B1
metabolism
polyketide synthase A is a multidomain PKS central to the biosynthesis of aflatoxin B1, a potent environmental carcinogen
metabolism
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the the norsolorinic acid anthrone-producing polyketide synthase, PksA, is involved in the aflatoxin biosynthetic pathway in Aspergillus parasiticus
metabolism
Aspergillus parasiticus SRRC 2043 / RHN1
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pksA is a polyketide synthase gene required for the early steps of aflatoxin biosynthesis
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the enzyme also has an editing function for the C-terminal thioesterase domain beyond its synthetic role in Claisen/Dieckmann cyclization and product release. Domain architecture and expected enzyme-bound intermediates of PksA, overview
additional information
the synthetic versatility of thioesterase domains in fungal nonreducing, iterative PKSs extends to Claisen cyclase chemistry by catalyzing C-C ring closure reactions as opposed to thioester hydrolysis or O-C/N-C macrocyclization observed in other thioesterase structures. Catalysis of C-C bond formation as a product release mechanism dramatically expands the synthetic potential of PKSs, structural analyses of the thioesterase/CLC domain in polyketide synthase A