Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (16)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Sayanova, O.
Right arrow Articles by Napier, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sayanova, O.
Right arrow Articles by Napier, J. A.
Agricola
Right arrow Articles by Sayanova, O.
Right arrow Articles by Napier, J. A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Experimental Botany, Vol. 52, No. 360, pp. 1581-1585, July 1, 2001
© 2001 Oxford University Press

Short Communications

Mutagenesis and heterologous expression in yeast of a plant {Delta}6-fatty acid desaturase

Olga Sayanova1, Frédéric Beaudoin1, Balázs Libisch1,2, Aude Castel1,3, Peter R. Shewry1 and Johnathan A. Napier1,4

1 IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS41 9AF, UK
2 Department of Plant Anatomy, Eötvös Loránd University, Budapest, Hungary
3 University Paris Sud, CNRS, F-91405 Orsay, France

Abstract

Membrane-bound microsomal fatty acid desaturases are known to have three conserved histidine boxes, comprising a total of up to eight histidine residues. Recently, a number of deviations from this consensus have been reported, with the substitution of a glutamine for the first histidine residue of the third histidine box being present in the so called ‘front end’ desaturases. These enzymes are also characterized by the presence of a cytochrome b5 domain at the protein N-terminus. Site-directed mutagenesis has been used to probe the functional importance of a number of amino acid residues which comprise the third histidine box of a ‘front end’ desaturase, the borage {Delta}6-fatty acid desaturase. This showed that the variant glutamine in the third histidine box is essential for enzyme activity and that histidine is not able to substitute for this residue.

Key words: Microsomal fatty acid desaturase, ‘front end’ desaturation, borage.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. Kaewsuwan, E. B. Cahoon, P.-F. Perroud, C. Wiwat, N. Panvisavas, R. S. Quatrano, D. J. Cove, and N. Bunyapraphatsara
Identification and Functional Characterization of the Moss Physcomitrella patens {Delta}5-Desaturase Gene Involved in Arachidonic and Eicosapentaenoic Acid Biosynthesis
J. Biol. Chem., August 4, 2006; 281(31): 21988 - 21997.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. J. Sasata, D. W. Reed, M. C. Loewen, and P. S. Covello
Domain Swapping Localizes the Structural Determinants of Regioselectivity in Membrane-bound Fatty Acid Desaturases of Caenorhabditis elegans
J. Biol. Chem., September 17, 2004; 279(38): 39296 - 39302.
[Abstract] [Full Text] [PDF]

Home page
 ANN BOT (LOND)Home page
T. M. DUNN, D. V. LYNCH, L. V. MICHAELSON, and J. A. NAPIER
A Post-genomic Approach to Understanding Sphingolipid Metabolism in Arabidopsis thaliana
Ann. Bot., May 1, 2004; 93(5): 483 - 497.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.