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The  S. cerevisiae PAD1  gene had been suggested to code for a cinnamic acid decarboxylase, converting  trans -cinnamic acid to styrene. This was suggested for the reason that the over-expression of  PAD1  resulted in increased tolerance toward cinnamic acid, up to 0.6 mM. We show that by over-expression of the  PAD1  together with the  FDC1  the cinnamic acid decarboxylase activity can be increased significantly. The strain over-expressing  PAD1  and  FDC1  tolerated cinnamic acid concentrations up to 10 mM. The cooperation of Pad1p and Fdc1p is surprising since the  PAD1  has a mitochondrial targeting sequence and the  FDC1  codes for a cytosolic protein. The cinnamic acid decarboxylase activity was also seen in the cell free extract. The activity was 0.019 μmol per minute and mg of extracted protein. The overexpression of  PAD1  and  FDC1  resulted also in increased activity with the hydroxycinnamic acids ferulic acid, p-coumaric acid and caffeinic acid. This activity was not seen when  FDC1  was overexpressed alone.  An efficient cinnamic acid decarboxylase is valuable for the genetic engineering of yeast strains producing styrene. Styrene can be produced from endogenously produced L-phenylalanine which is converted by a phenylalanine ammonia lyase to cinnamic acid and then by a decarboxylase to styrene.

Overexpression of PAD1 and FDC1 results in significant cinnamic acid decarboxylase activity in Saccharomyces cerevisiae