Document Detail

Plant fatty acyl reductases: Enzymes generating fatty alcohols for protective layers with potential for industrial applications.
MedLine Citation:
PMID:  22794916     Owner:  NLM     Status:  In-Data-Review    
Primary fatty alcohols are found throughout the biological world, either in free form or in a combined state. They are common components of plant surface lipids (i.e. cutin, suberin, sporopollenin, and associated waxes) and their absence can significantly perturb these essential barriers. Fatty alcohols and/or derived compounds are also likely to have direct functions in plant biotic and abiotic interactions. An evolutionarily related set of alcohol-forming fatty acyl reductases (FARs) is present in all kingdoms of life. Plant microsomal and plastid-associated FAR enzymes have been characterized, acting on acyl-coenzymeA (acyl-CoA) or acyl-acyl carrier protein (acyl-ACP) substrates, respectively. FARs have distinct substrate specificities both with regard to chain length and chain saturation. Fatty alcohols and wax esters, which are a combination of fatty alcohol and fatty acid, have a variety of commercial applications. The expression of FARs with desired specificities in transgenic microbes or oilseed crops would provide a novel means of obtaining these valuable compounds. In the present review, we report on recent progress in characterizing plant FAR enzymes and in understanding the biological roles of primary fatty alcohols, as well as describe the biotechnological production and industrial uses of fatty alcohols.
Owen Rowland; Frédéric Domergue
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Publication Detail:
Type:  Journal Article     Date:  2012-05-16
Journal Detail:
Title:  Plant science : an international journal of experimental plant biology     Volume:  193-194     ISSN:  1873-2259     ISO Abbreviation:  Plant Sci.     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-07-16     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882015     Medline TA:  Plant Sci     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  28-38     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ireland Ltd. All rights reserved.
Department of Biology and Institute of Biochemistry, Carleton University, Ottawa, Ontario, K1S 5B6, Canada.
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