Tomato phenylacetaldehyde reductases catalyze the last step in the synthesis of the aroma volatile 2-phenylethanol
2007
Tieman, D.M. | Loucas, H.M. | Kim, J.Y. | Clark, D.G. | Klee, H.J.
The volatile compounds, 2-phenylacetaldehyde and 2-phenylethanol, are important for the aroma and flavor of many foods, such as ripe tomato fruits, and are also major constituents of scent of many flowers, most notably roses. While much work has gone into elucidating the pathway for 2-phenylethanol synthesis in bacteria and yeast, the pathways for synthesis in plants are not well characterized. We have identified two tomato enzymes (LePAR1 and LePAR2) that catalyze the conversion of 2-phenylacetaldehyde to 2-phenylethanol: LePAR1, a member of the large and diverse short-chain dehydrogenase/reductase family, strongly prefers 2-phenylacetaldehyde to its shorter and longer homologues (benzaldehyde and cinnamaldehyde, respectively) and does not catalyze the reverse reaction at a measurable rate; LePAR2, however, has similar affinity for 2-phenylacetaldehyde, benzaldehyde and cinnamaldehyde. To confirm the activity of these enzymes in vivo, LePAR1 and LePAR2 cDNAs were individually expressed constitutively in petunia. While wild type petunia flowers emit relatively high levels of 2-phenylacetaldehyde and lower levels of 2-phenylethanol, flowers from the transgenic plants expressing LePAR1 or LePAR2 had significantly higher levels of 2-phenylethanol and lower levels of 2-phenylacetaldehyde. The in vivo alteration of volatile emissions is an important step toward altering aroma volatiles in plants.
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