Literature summary for 2.3.1.221 extracted from

Crawford, J.M.; Korman, T.P.; Labonte, J.W.; Vagstad, A.L.; Hill, E.A.; Kamari-Bidkorpeh, O.; Tsai, S.C.; Townsend, C.A.
Structural basis for biosynthetic programming of fungal aromatic polyketide cyclization (2009), Nature, 461, 1139-1143.

Search for more literature for 2.3.1.221

Cloned(Commentary)

Cloned (Comment)	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	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]	Aspergillus parasiticus	-	7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Aspergillus parasiticus	-	gene pksA	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant proteins from Escherichia coli strains BL21(DE3) or Rosetta2(DE3)	Aspergillus parasiticus

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7 malonyl-CoA + hexanoyl-[acyl-carrier protein]	-	Aspergillus parasiticus	7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O	-	?

Subunits

Subunits	Comment	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

Synonyms

Synonyms	Comment	Organism
PksA	-	Aspergillus parasiticus

General Information

General Information	Comment	Organism
metabolism	biosynthesis of norsolorinic acid anthrone by PksA, detailed overview	Aspergillus parasiticus

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Release 2023.1 (January 2023)