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Literature summary for 2.3.1.B25 extracted from

  • Watanabe, K.; Praseuth, A.P.; Wang, C.C.
    A comprehensive and engaging overview of the type III family of polyketide synthases (2007), Curr. Opin. Chem. Biol., 11, 279-286.
    View publication on PubMed
Search for more literature for 2.3.1.B25

Application

Application Comment Organism
molecular biology use of octaketide synthase for rational biosynthetic engineering to generate molecular diversity and pursue innovative, biologically potent compounds Aloe arborescens

Protein Variants

Protein Variants Comment Organism
G197A site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing heptaketides Aloe arborescens
G197T site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing hexaketides Aloe arborescens
G197W site-directed mutagenesis, the mutant enzyme shows altered activity compared to the wild-type enzyme producing tri- and pentaketides Aloe arborescens
additional information generation molecularly diverse plant type III polyketides through rational engineering of the oktaketide synthase active site Aloe arborescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
8 malonyl-CoA Aloe arborescens
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 8 CoA + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one + 8 CO2 + H2O
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 ?
additional information Aloe arborescens the oktaketide synthase reaction is also catalyzed by chalcone synthase (EC 2.3.1.74) mutant T197G/G256L/S338V, CHS containing a double point mutation G256L/S338V not only accepts 4coumaroyl-CoA but also biosynthesizes octaketides SEK4 and 4b, exhausting eight malonyl-CoAs ?
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 ?

Organism

Organism UniProt Comment Textmining
Aloe arborescens Q3L7F5 single gene
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
8 malonyl-CoA
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 Aloe arborescens 8 CoA + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one + 8 CO2 + H2O
-
 ?
8 malonyl-CoA
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 Aloe arborescens 8 CoA + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one + 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one + 8 CO2 + H2O i.e. SEK4 and SEK4b ?
additional information the oktaketide synthase reaction is also catalyzed by chalcone synthase (EC 2.3.1.74) mutant T197G/G256L/S338V, CHS containing a double point mutation G256L/S338V not only accepts 4coumaroyl-CoA but also biosynthesizes octaketides SEK4 and 4b, exhausting eight malonyl-CoAs Aloe arborescens ?
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 ?

Synonyms

Synonyms Comment Organism
OKS
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 Aloe arborescens
oktaketide synthase
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 Aloe arborescens

General Information

General Information Comment Organism
evolution pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases Aloe arborescens
additional information active site structure of wild-type and mutant enzymes, overview. Amino acid residue at position 197 in the active site governs the chain length of the polyketide. Leucine at position 256 in the active site for both OKS and PCS influences the substrate preference for malonyl-CoA as a starting unit, while a glycine residue located in the same position and found in the catalytic pocket of chalcone synthase can possibly compel the enzyme to readily accept 4-coumaroyl-CoA as a starting unit Aloe arborescens