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- W2468615650 abstract "A growing number of functionally divergent type III polyketide synthases (PKSs), the chalcone synthase (CHS) superfamily enzymes, have been cloned and characterized, which include recently obtained pentaketide chromone synthase (PCS) and octaketide synthase (OKS) from aloe (Aloe arborescens). Recombinant PCS expressed in Escherichia coli catalyzed successive condensations of malonyl-CoA to produce a pentaketide, 5,7-dihydroxy-2-methylchromone, while recombinant OKS yielded octaketides, SEK4 and SEK4b, the longest polyketides produced by the structurally simple type III PKS. PCS and OKS share 91% amino acid sequence identity, and maintain the conserved Cys-His-Asn catalytic triad. The most characteristic feature is that the CHS active-site residue 197 (numbering in Medicago sativa CHS) is uniquely replaced with Met in PCS and Gly in OKS, respectively. Site-directed mutagenesis revealed that the steric bulk of the chemically inert residue lining the active-site cavity determines the polyketide chain length and the product specificity." @default.
- W2468615650 created "2016-07-22" @default.
- W2468615650 creator A5045857743 @default.
- W2468615650 date "2007-01-11" @default.
- W2468615650 modified "2023-09-26" @default.
- W2468615650 title "Engineered Biosynthesis of Plant Polyketides: Chain Length Control in Novel Type III Polyketide Synthases" @default.
- W2468615650 doi "https://doi.org/10.1021/bk-2007-0955.ch008" @default.
- W2468615650 hasPublicationYear "2007" @default.
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