4-Hydroxycinnamoyl-CoA hydratase/lyase, an enzyme of phenylpropanoid cleavage from Pseudomonas, causes formation of C6-C1 acid and alcohol glucose conjugates when expressed in hairy roots of Datura stramonium L.

Adinpunya Mitra, Melinda J. Mayer, Fred A. Mellon, Anthony J. Michael, Arjan Narbad, Adrian J. Parr, Keith W. Waldron, Nicholas J. Walton

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45 Scopus citations


4-Hydroxycinnamoyl-CoA hydratase/lyase (HCHL), a crotonase homologue of phenylpropanoid catabolism from Pseudomonas fluorescens strain AN103, led to the formation of 4-hydroxybenzaldehyde metabolites when expressed in hairy root cultures of Datura stramonium L. established by transformation with Agrobacterium rhizogenes. The principal new compounds observed were the glucoside and glucose ester of 4-hydroxybenzoic acid, together with 4-hydroxybenzyl alcohol-O-β-D-glucoside. In lines actively expressing HCHL, these together amounted to around 0.5% of tissue fresh mass. No protocatechuic derivatives were found, although a trace of vanillic acid-β-D-glucoside was detected. There was no accumulation of 4-hydroxybenzaldehydes, whether free or in the form of their glucose conjugates. There was some evidence suggesting a diminished availability of feruloyl-CoA for the production of feruloyl putrescine and coniferyl alcohol. The findings are discussed in the context of a diversion of phenylpropanoid metabolism, and the ability of plants and plant cultures to conjugate phenolic compounds.

Original languageEnglish (US)
Pages (from-to)79-89
Number of pages11
Issue number1
StatePublished - Dec 1 2002



  • 4-Hydroxycinnamoyl-CoA hydratase/lyase
  • Datura (phenylpropanoid metabolism)
  • Glucoside
  • Hydroxybenzaldehyde
  • Phenylpropanoid metabolism
  • Vanillin

ASJC Scopus subject areas

  • Genetics
  • Plant Science

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