title: Enzymatic formation of unnatural aromatic polyketides by chalcone synthase.
abstract: Substrate specificity of recombinant chalcone synthase (CHS) from Scutellaria baicalensis (Labiatae) was investigated using chemically synthesized aromatic and aliphatic CoA esters. It was demonstrated for the first time that CHS converted benzoyl-CoA to phlorobenzophenone (2,4,6-trihydroxybenzophenone) along with pyrone by-products. On the other hand, phenylacetyl-CoA was enzymatically converted to an unnatural aromatic polyketide, phlorobenzylketone (2, 4,6-trihydroxyphenylbenzylketone), whose structure was finally confirmed by chemical synthesis. Furthermore, in agreement with earlier reports, S. baicalensis CHS also accepted aliphatic CoA esters, isovaleryl-CoA and isobutyryl-CoA, to produce phloroacylphenones. In contrast, hexanoyl-CoA only afforded pyrone derivatives without formation of a new aromatic ring. It was noteworthy that both aromatic and aliphatic CoA esters were accepted in the active site of the enzyme as a starter substrate for the complex condensation reaction. The low substrate specificity of CHS thus provided further insight into the structure and function of the enzyme.
authors: School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka, 422-8526, Japan.
authors: H
authors: H
authors: Morita
authors: Y
authors: Y
authors: Takahashi
authors: H
authors: H
authors: Noguchi
authors: I
authors: I
authors: Abe
mesh_terms: D000217:Acyltransferases / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D019684:Magnoliopsida / Q000201:enzymology; D011994:Recombinant Proteins / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization
chemical_list: D011994:Recombinant Proteins; D000217:Acyltransferases; C020141:flavanone synthetase