Distribution and activity of microsomal NADPH-dependent monooxygenases and amino acid decarboxylases in cruciferous and non-cruciferous plants, and their relationship to foliar glucosinolate content

A - Papers appearing in refereed journals

Bennett, R. N., Kiddle, G., Hick, A. J., Dawson, G. W. and Wallsgrove, R. M. 1996. Distribution and activity of microsomal NADPH-dependent monooxygenases and amino acid decarboxylases in cruciferous and non-cruciferous plants, and their relationship to foliar glucosinolate content. Plant, Cell and Environment. 19 (7), pp. 801-812.

AuthorsBennett, R. N., Kiddle, G., Hick, A. J., Dawson, G. W. and Wallsgrove, R. M.
Abstract

The NADPH-dependent conversion of amino acids to their aldoximes is an initial step in glucosinolate biosynthesis. A number of microsomal aldoxime-forming monooxygenase activities were detected in leaves from a variety of glucosinolate-containing species, whereas barley, bean and tobacco leaves did not contain any such activities. The substrates for these monooxygenases in each species largely correlated with the spectrum of glucosinolates found in that species. No activity was detected that metabolized homomethionine (supposed precursor of 2-propenylglucosinolate [sinigrin]), even in species where sinigrin was the major glucosinolate. Zn Sinapis species containing hydroxybenzylglucosinolate (sinalbin), activity with L-Tyr was detected, whereas Brassica species containing sinalbin had no such activity. However, these Brassicas did contain an L-Phe monooxygenase activity. Partial characterization of the monooxygenases indicated that in Brassica species, Nasturtium officinalis and Raphanus sativus these resembled the flavin-linked monooxygenases previously found in oilseed rape (Brassica napus) and Chinese cabbage (Brassica campestris). The L-Tyr-dependent activity in Sinapis species, and the L-Phe-dependent activity in Tropaeolum majus, had characteristics of cytochrome P450-type enzymes. No similarity was found with any other known amino acid metabolizing enzymes (including decarboxylases, amino acid oxidases and diamine/polyamine oxidases).

KeywordsPlant Sciences
Year of Publication1996
JournalPlant, Cell and Environment
Journal citation19 (7), pp. 801-812
Digital Object Identifier (DOI)doi:10.1111/j.1365-3040.1996.tb00417.x
Open accessPublished as non-open access
Funder project or code905
215
236
413
437
Project: 011281
ISSN01407791
PublisherWiley

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