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Literature summary extracted from

  • Vagstad, A.L.; Bumpus, S.B.; Belecki, K.; Kelleher, N.L.; Townsend, C.A.
    Interrogation of global active site occupancy of a fungal iterative polyketide synthase reveals strategies for maintaining biosynthetic fidelity (2012), J. Am. Chem. Soc., 134, 6865-6877.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.221 expression of N-terminally His6-tagged enzyme domains in Escherichia coli strain BL21(DE3) Aspergillus parasiticus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.221 S1937A inactive mutant Aspergillus parasiticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.221 1.46
-
 hexanoyl-[acyl-carrier protein] pH 7.0, 22°C Aspergillus parasiticus
2.3.1.221 15.38
-
 acetyl-[acyl-carrier protein] pH 7.0, 22°C Aspergillus parasiticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.221 7 malonyl-CoA + hexanoyl-[acyl-carrier protein] Aspergillus parasiticus
-
 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.221 Aspergillus parasiticus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.221 recombinant N-terminally His6-tagged enzyme domains from Escherichia coli strain BL21(DE3) Aspergillus parasiticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.221 7 malonyl-CoA + acetyl-[acyl-carrier protein]
-
 Aspergillus parasiticus ?
-
 ?
2.3.1.221 7 malonyl-CoA + hexanoyl-[acyl-carrier protein]
-
 Aspergillus parasiticus 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
 ?
2.3.1.221 7 malonyl-CoA + hexanoyl-[acyl-carrier protein] ACP-bound intermediates and major products of the reaction, overview Aspergillus parasiticus 7 CoA + norsolorinic acid anthrone + [acyl-carrier protein] + 7 CO2 + 2 H2O
-
 ?
2.3.1.221 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 Aspergillus parasiticus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.221 More PksA domain structure, from N- to C-terminus including the starter unit: acylcarrier protein transacylase (SAT), beta-ketoacyl synthase (KS), malonyl-CoA: acyl-carrier protein transacylase (MAT), product template (PT), acyl-carrier protein (ACP), and thioesterase/Claisen cyclase (TE/CLC) Aspergillus parasiticus

Synonyms

EC Number Synonyms Comment Organism
2.3.1.221 norsolorinic acid anthrone-producing polyketide synthase
-
 Aspergillus parasiticus
2.3.1.221 PksA
-
 Aspergillus parasiticus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.221 22
-
 assay at room temperature Aspergillus parasiticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.221 0.0407
-
 acetyl-[acyl-carrier protein] pH 7.0, 22°C Aspergillus parasiticus
2.3.1.221 0.0472
-
 hexanoyl-[acyl-carrier protein] pH 7.0, 22°C Aspergillus parasiticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.221 7
-
 assay at Aspergillus parasiticus

General Information

EC Number General Information Comment Organism
2.3.1.221 metabolism the the norsolorinic acid anthrone-producing polyketide synthase, PksA, is involved in the aflatoxin biosynthetic pathway in Aspergillus parasiticus Aspergillus parasiticus
2.3.1.221 additional information 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 Aspergillus parasiticus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.221 0.0026
-
 acetyl-[acyl-carrier protein] pH 7.0, 22°C Aspergillus parasiticus
2.3.1.221 0.032
-
 hexanoyl-[acyl-carrier protein] pH 7.0, 22°C Aspergillus parasiticus