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Biochem Biophys Res Commun. 2004 Dec 10;325(2):561-7.

Probing biosynthesis of plant polyketides with synthetic N-acetylcysteamine thioesters.

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  • 1School of Pharmaceutical Sciences, and the 21st Century COE Program, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526, Japan.


Recombinant chalcone synthase (CHS) from Scutellaria baicalensis accepted cinnamoyl diketide-NAC and cinnamoyl-NAC as a substrate, and carried out sequential condensations with malonyl-CoA to produce 2',4',6'-trihydroxychalcone. Steady-state kinetic analysis revealed that the CHS accepted the diketide-NAC with less efficiency, while cinnamoyl-NAC primed the enzyme reaction almost as efficiently as cinnamoyl-CoA. On the other hand, it was for the first time demonstrated that the diketide-NAC was also a substrate for recombinant polyketide reductase (PKR) from Glycyrrhiza echinata, and converted to the corresponding beta-ketohemithioester. Furthermore, by co-action of the CHS and the PKR, the NAC-thioesters were converted to 6'-deoxychalcone in the presence of NADPH and malonyl-CoA.

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