Plant Physiol. Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (27)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bennett, R.
Right arrow Articles by Wallsgrove, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bennett, R.
Right arrow Articles by Wallsgrove, R.
Agricola
Right arrow Articles by Bennett, R.
Right arrow Articles by Wallsgrove, R.

PLANT PHYSIOLOGY , Vol 102, Issue 4 1307-1312, Copyright © 1993 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Aldoxime-Forming Microsomal Enzyme Systems Involved in the Biosynthesis of Glucosinolates in Oilseed Rape (Brassica napus) Leaves

R. Bennett, A. Donald, G. Dawson, A. Hick and R. Wallsgrove
Biochemistry and Physiology Department (R.B., A.D., R.W.) and Biological and Ecological Chemistry Department (G.D., A.H.), Institute for Arable Crops Research Rothamsted Experimental Station, Harpenden AL5 2JQ, United Kingdom

Glucosinolates and cyanogenic glucosides are synthesized from amino acids via similar intermediates, N-hydroxyamino acids and aldoximes. Microsomal preparations from young green leaves of oilseed rape catalyze the NADPH-dependent metabolism of homo-phenylalanine and dihomomethionine to the respective aldoximes, precursors of 2-phenylethyl and 3-butenyl glucosinolates. Cytochrome P-450-type enzymes are not involved (in contrast to cyanogenic glucoside biosynthesis), because neither activity was affected by carbon monoxide or other cytochrome P-450 inhibitors. Copper ions and diethyl pyrocarbonate were potent inhibitors of the enzymes, and treatment of microsomes with detergents abolished the overall activity. Two distinct enzyme systems with similar properties appear to be involved, each specific for a particular substrate. One utilizes dihomomethionine and is not active with homophenylalanine or any other amino acid tested, and the other is specific for homophenylalanine. From the characteristics of these enzymes, it seems that these early steps in glucosinolate biosynthesis may be catalyzed by flavin-containing monooxygenases comparable to those found in mammalian tissues and elsewhere. The pathways for the biosynthesis of glucosinolates and cyanogenic glucosides have apparently evolved independently, despite the similar chemical conversions involved.


This article has been cited by other articles:


Home page
 Plant CellHome page
B. Reintanz, M. Lehnen, M. Reichelt, J. Gershenzon, M. Kowalczyk, G. Sandberg, M. Godde, R. Uhl, and K. Palme
bus, a Bushy Arabidopsis CYP79F1 Knockout Mutant with Abolished Synthesis of Short-Chain Aliphatic Glucosinolates
PLANT CELL, February 1, 2001; 13(2): 351 - 367.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
U. Wittstock and B. A. Halkier
Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. Catalyzes the Conversion of L-Phenylalanine to Phenylacetaldoxime in the Biosynthesis of Benzylglucosinolate
J. Biol. Chem., May 5, 2000; 275(19): 14659 - 14666.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. D. Mikkelsen, C. H. Hansen, U. Wittstock, and B. A. Halkier
Cytochrome P450 CYP79B2 from Arabidopsis Catalyzes the Conversion of Tryptophan to Indole-3-acetaldoxime, a Precursor of Indole Glucosinolates and Indole-3-acetic Acid
J. Biol. Chem., October 20, 2000; 275(43): 33712 - 33717.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. H. Hansen, U. Wittstock, C. E. Olsen, A. J. Hick, J. A. Pickett, and B. A. Halkier
Cytochrome P450 CYP79F1 from Arabidopsis Catalyzes the Conversion of Dihomomethionine and Trihomomethionine to the Corresponding Aldoximes in the Biosynthesis of Aliphatic Glucosinolates
J. Biol. Chem., March 30, 2001; 276(14): 11078 - 11085.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1993 by the American Society of Plant Biologists