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


     


This Article
Right arrow Full Text
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 (52)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Robineau, T.
Right arrow Articles by Werck-Reichhart, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Robineau, T.
Right arrow Articles by Werck-Reichhart, D.
Agricola
Right arrow Articles by Robineau, T.
Right arrow Articles by Werck-Reichhart, D.

The Chemically Inducible Plant Cytochrome P450 CYP76B1 Actively Metabolizes Phenylureas and Other Xenobiotics1

Tiburce Robineau, Yannick Batard, Svetlana Nedelkina, Francisco Cabello-Hurtado, Monique LeRet, Odile Sorokine, Luc Didierjean, and Danièle Werck-Reichhart*

Département d'Enzymologie Cellulaire et Moléculaire, Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique Unité Propre de Recherche 406, 28 rue Goethe, F-67000 Strasbourg, France (T.R., Y.B., F.C.-H., M.L., L.D., D.W.-R.); Institute of Cytology and Genetics, 630090 Novosibirsk-90, Russia (S.N.); and Laboratoire de Spectrométrie de Masse Bioorganique, Centre National de la Recherche Scientifique-Unité Mixte de Recherche 7509, 1 rue Blaise Pascal F-67000 Strasbourg, France (O.S.)

Cytochrome P450s (P450s) constitute one of the major classes of enzymes that are responsible for detoxification of exogenous molecules both in animals and plants. On the basis of its inducibility by exogenous chemicals, we recently isolated a new plant P450, CYP76B1, from Jerusalem artichoke (Helianthus tuberosus) and showed that it was capable of dealkylating a model xenobiotic compound, 7-ethoxycoumarin. In the present paper we show that CYP76B1 is more strongly induced by foreign compounds than other P450s isolated from the same plant, and metabolizes with high efficiency a wide range of xenobiotics, including alkoxycoumarins, alkoxyresorufins, and several herbicides of the class of phenylureas. CYP76B1 catalyzes the double N-dealkylation of phenylureas with turnover rates comparable to those reported for physiological substrates and produces nonphytotoxic compounds. Potential uses for CYP76B1 thus include control of herbicide tolerance and selectivity, as well as soil and groundwater bioremediation.


1   This work was supported in part by the Convention Groupement de Recherches et d'Etudes sur les Génomes/Institut National de la Recherche Agronomique "Complémentation de la levure par des gènes de plantes." Y.B. was supported by the Ministère de la Recherche et de l'Enseignement Supérieur, S.N. by a fellowship in toxicology from the European Science Foundation, and F.C.H. by a postdoctoral grant from the Spanish Ministerio de Agricultura, Pesca y Alimentacíon.
*   Corresponding author; e-mail daniele.werck{at}ibmp-ulp.u-strasbg.fr; fax 33-3-88-35-84-84.

Plant Physiol. (1998) 118: 1049-1056
Copyright Clearance Center:   0032-0889/98/118//08
© 1998 American Society of Plant Physiologists




This article has been cited by other articles:


Home page
Plant Physiol.Home page
G. A. Schoch, R. Attias, M. Belghazi, P. M. Dansette, and D. Werck-Reichhart
Engineering of a Water-Soluble Plant Cytochrome P450, CYP73A1, and NMR-Based Orientation of Natural and Alternate Substrates in the Active Site
Plant Physiology, November 1, 2003; 133(3): 1198 - 1208.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
L. Didierjean, L. Gondet, R. Perkins, S.-M. C. Lau, H. Schaller, D. P. O'Keefe, and D. Werck-Reichhart
Engineering Herbicide Metabolism in Tobacco and Arabidopsis with CYP76B1, a Cytochrome P450 Enzyme from Jerusalem Artichoke
Plant Physiology, September 1, 2002; 130(1): 179 - 189.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
M. W. Persans, J. Wang, and M. A. Schuler
Characterization of Maize Cytochrome P450 Monooxygenases Induced in Response to Safeners and Bacterial Pathogens
Plant Physiology, February 1, 2001; 125(2): 1126 - 1138.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
B. Siminszky, F. T. Corbin, E. R. Ward, T. J. Fleischmann, and R. E. Dewey
Expression of a soybean cytochrome P450 monooxygenase cDNA in yeast and tobacco enhances the metabolism of phenylurea herbicides
PNAS, February 16, 1999; 96(4): 1750 - 1755.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. O. Latunde-Dada, F. Cabello-Hurtado, N. Czittrich, L. Didierjean, C. Schopfer, N. Hertkorn, D. Werck-Reichhart, and J. Ebel
Flavonoid 6-Hydroxylase from Soybean (Glycine max L.), a Novel Plant P-450 Monooxygenase
J. Biol. Chem., January 12, 2001; 276(3): 1688 - 1695.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1998 by the American Society of Plant Biologists