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Acyltransferase-catalysed p-coumarate ester formation is a committed step of lignin biosynthesis

, , , , , , & show all
Pages 50-53 | Published online: 21 Feb 2007
 

Abstract

An acyltransferase (HCT) catalyses the production of p-coumaroyl-shikimate/quinate esters, the substrates of the 3-hydroxylase involved in phenylpropanoid biosynthesis. The heterologously expressed enzyme was shown to transfer the acyl group of p-coumaroyl-CoA to shikimate or quinate. HCT gene silencing in Arabidopsis thaliana and Nicotiana benthamiana resulted in changes in lignin amount and composition, thus demonstrating HCT function in planta.

Acknowledgement

We thank Frédéric Legée (INRA) for Klason determinations.

Notes

CoA, coenzyme A; HCT, hydroxycinnamoyl-CoA : shikimate/quinate hydroxycinnamoyltransferase; TRV, tobacco rattle virus; VIGS, virus-induced gene silencing

Additional information

Notes on contributors

L Hoffmann

CoA, coenzyme A; HCT, hydroxycinnamoyl-CoA : shikimate/quinate hydroxycinnamoyltransferase; TRV, tobacco rattle virus; VIGS, virus-induced gene silencing

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