This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Minto, R. E.
Right arrow Articles by Pratt, A. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Minto, R. E.
Right arrow Articles by Pratt, A. C.
Agricola
Right arrow Articles by Minto, R. E.
Right arrow Articles by Pratt, A. C.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, February 2009, p. 1156-1164, Vol. 75, No. 4
0099-2240/09/$08.00+0     doi:10.1128/AEM.02049-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Atypical Biosynthetic Properties of a {Delta}12/{nu}+3 Desaturase from the Model Basidiomycete Phanerochaete chrysosporium{triangledown} ,{dagger}

Robert E. Minto,* Brenda J. Blacklock, Hina Younus, and Andrew C. Pratt

Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202

Received 3 September 2008/ Accepted 7 December 2008

The model white-rot basidiomycete Phanerochaete chrysosporium contains a single integral membrane {Delta}12-desaturase FAD2 related to the endoplasmic reticular plant FAD2 enzymes. The fungal fad2-like gene was cloned and distinguished itself from plant homologs by the presence of four introns and a significantly larger coding region. The coding sequence exhibits ca. 35% sequence identity to plant homologs, with the highest sequence conservation found in the putative catalytic and major structural domains. In vivo activity of the heterologously expressed enzyme favors C18 substrates with {nu}+3 regioselectivity, where the site of desaturation is three carbons carboxy-distal to the reference position of a preexisting double bond ({nu}). Linoleate accumulated to levels in excess of 12% of the total fatty acids upon heterologous expression of P. chrysosporium FAD2 in Saccharomyces cerevisiae. In contrast to the behavior of the plant FAD2 enzymes, this oleate desaturase does not 12-hydroxylate lipids and is the first example whose activity increases at higher temperatures (30°C versus 15°C). Thus, while maintaining the hallmark activity of the fatty acyl {Delta}12-desaturase family, the basidiomycete fad2 genes appear to have evolved substantially from an ancestral desaturase.


* Corresponding author. Mailing address: Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, 402 N. Blackford St., LD 326, Indianapolis, IN 46202. Phone: (317) 274-6869. Fax: (317) 274-4701. E-mail: rminto{at}iupui.edu

{triangledown} Published ahead of print on 16 December 2008.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.


Applied and Environmental Microbiology, February 2009, p. 1156-1164, Vol. 75, No. 4
0099-2240/09/$08.00+0     doi:10.1128/AEM.02049-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.