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Planta

, Volume 196, Issue 2, pp 239–244 | Cite as

Developmental regulation of aldoxime formation in seedlings and mature plants of Chinese cabbage (Brassica campestris ssp. pekinensis) and oilseed rape (Brassica napus): Glucosinolate and IAA biosynthetic enzymes

  • Richard Bennett
  • Jutta Ludwig-Muller
  • Guy Kiddle
  • Willy Hilgenberg
  • Roger Wallsgrove
Article

Abstract

The first steps in the biosynthesis of glucosinolates and indole-3-acetic acid (IAA) in oilseed rape (Brassica napus L.) and Chinese cabbage (Brassica campestris ssp. pekinensis) involve the formation of aldoximes. In rape the formation of aldoximes from chain-extended amino acids, for aromatic and aliphatic glucosinolate biosynthesis, is catalysed by microsomal flavin-containing monooxygenases. The formation of indole-3-aldoxime from l-tryptophan, the potential precursor of both indole-3-acetic acid and indolyl-glucosinolates, is catalysed by several microsomal peroxidases. The biosynthesis of glucosinolates and indole-3-acetic acid was shown to be under developmental control in oilseed rape and Chinese cabbage. No monooxygenase activities were detected in cotyledons or old leaves of either species. The highest monooxygenase activities were found in young expanding leaves; as the leaves reached full expansion and matured the activities decreased rapidly. The indole-aldoxime-forming activity was found in all of the tissues analysed, but there was also a clear decrease in foliar activity with maturity in leaves of rape and Chinese cabbage. Partial characterisation of the Chinese cabbage monooxygenases showed that they have essentially identical properties to the previously characterised rape enzymes; they are not cytochrome P450-type enzymes, but resemble flavin-containing monooxygenases. No monooxygenase inhibitors were detected in microsomes prepared from either cotyledons or old leaves.

Key words

Aldoxime biosynthesis Auxin biosynthesis Brassica Glucosinolate 

Abbreviations

DHMet

dihomomethionine

FMO

flavin-containing monooxygenase

HPhe

homophenylalanine

IAA

indole-3-acetic acid

l-Phe

l-phenylalanine

l-Trp

l-tryptophan

MO

monooxygenase

IAALD

indole-3-acetaldehyde

IAOX

indole-3-aldoxime

THMet

trihomomethionine

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Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • Richard Bennett
    • 1
  • Jutta Ludwig-Muller
    • 2
  • Guy Kiddle
    • 1
  • Willy Hilgenberg
    • 2
  • Roger Wallsgrove
    • 1
  1. 1.Biochemistry & Physiology DepartmentIACR Rothamsted Experimental StationHarpendenUK
  2. 2.Botanisches Institut, J.W. Goethe UniversitätFrankfurt am Main 11Germany

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