Enzymatic formation of an unnatural C(6)-C(5) aromatic polyketide by plant type III polyketide synthases.
[reaction: see text] Substrate specificities of plant polyketide synthases (PKSs) were investigated using analogues of malonyl-CoA, the extension unit of the polyketide chain elongation reactions. When incubated with methylmalonyl-CoA and 4-coumaroyl-CoA, plant PKSs (chalcone synthase from Scutellaria baicalensis, stilbene synthase from Arachis hypogaea, and benzalacetone synthase from Rheum palmatum) afforded an unnatural C(6)-C(5) aromatic polyketide, 1-(4-hydroxyphenyl)pent-1-en-3-one, formed by one-step decarboxylative condensation of the two substrates. In contrast, succinyl-CoA was not accepted as a substrate by the enzymes.
Abe
Ikuro
I
University of Shizuoka, School of Pharmaceutical Sciences, 52-1 Yada, Shizuoka 422-8526, Japan. abei@ys7.u-shizuoka-ken.ac.jp
Takahashi
Yusuke
Y
Noguchi
Hiroshi
H
D002074:Butanones / Q000378:metabolism; D002599:Chalcone / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D019684:Magnoliopsida / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D013267:Stilbenes / Q000378:metabolism; D013379:Substrate Specificity
D002074:Butanones; D009097:Multienzyme Complexes; D013267:Stilbenes; D002599:Chalcone; C025383:benzylideneacetone