Versatility in acyltransferase activity completes chicoric acid biosynthesis in purple coneflower

Rao Fu, Pingyu Zhang, Ge Jin, Lianglei Wang, Shiqian Qi, Yang Cao, Cathie Martin and Yang Zhang ()
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Rao Fu: Sichuan University
Pingyu Zhang: Sichuan University
Ge Jin: Sichuan University
Lianglei Wang: Sichuan University
Shiqian Qi: Sichuan University, and Collaborative Innovation Center for Biotherapy
Yang Cao: Sichuan University
Cathie Martin: Department of Metabolic Biology and Biological Chemistry, John Innes Centre
Yang Zhang: Sichuan University

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: Abstract Purple coneflower (Echinacea purpurea (L.) Moench) is a popular native North American herbal plant. Its major bioactive compound, chicoric acid, is reported to have various potential physiological functions, but little is known about its biosynthesis. Here, taking an activity-guided approach, we identify two cytosolic BAHD acyltransferases that form two intermediates, caftaric acid and chlorogenic acid. Surprisingly, a unique serine carboxypeptidase-like acyltransferase uses chlorogenic acid as its acyl donor and caftaric acid as its acyl acceptor to produce chicoric acid in vacuoles, which has evolved its acyl donor specificity from the better-known 1-O-β-D-glucose esters typical for this specific type of acyltransferase to chlorogenic acid. This unusual pathway seems unique to Echinacea species suggesting convergent evolution of chicoric acid biosynthesis. Using these identified acyltransferases, we have reconstituted chicoric acid biosynthesis in tobacco. Our results emphasize the flexibility of acyltransferases and their roles in the evolution of specialized metabolism in plants.

Date: 2021
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DOI: 10.1038/s41467-021-21853-6

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