Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052802 | FEBS Letters | 2005 | 5 Pages |
Abstract
The Δ6-fatty acid desaturase is a key enzyme in the synthesis of an important fatty acid, γ-linolenic acid. We have characterized, by heterologous expression in Saccharomyces cerevisiae, substrate specificity and preference of Δ6-desaturase of Mucor rouxii. Fatty acid supplementation was carried out based on the predicted enzyme topology, fatty acid phenotype and the corresponding metabolic pathway in M. rouxii. The enzyme has a broad substrate specificity as based on C15–C18. The result also supported classification of the M. rouxii Δ6-desaturase into a front-end desaturase. Interestingly, a relatively rare activity based on odd acyl chains and not described previously in other eukaryotic Δ6-desaturases was also observed.
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Authors
Sutthicha Na-Ranong, Kobkul Laoteng, Prasat Kittakoop, Morakot Tantichareon, Supapon Cheevadhanarak,