4-Hydroxycinnamoyl-CoA hydratase/lyase,an enzyme of phenylpropanoid cleavage from Pseudomonas,causes formation of C(6)-C(1) acid and alcohol glucose conjugates when expressed in hairy roots of Datura stramonium L |
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Authors: | Mitra Adinpunya Mayer Melinda J Mellon Fred A Michael Anthony J Narbad Arjan Parr Adrian J Waldron Keith W Walton Nicholas J |
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Institution: | Food Safety Science Division, Institute of Food Research, Norwich Resesrch Park, Colney, Norwich NR4 7UA, UK. |
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Abstract: | 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-beta- 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-beta- 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. |
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