Targeted mutagenesis of a fatty acid Delta6-desaturase from Mucor rouxii: role of amino acid residues adjacent to histidine-rich motif II |
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Authors: | Na-Ranong Sutthicha Laoteng Kobkul Kittakoop Prasat Tanticharoen Morakot Cheevadhanarak Supapon |
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Institution: | School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand. |
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Abstract: | The amino acid residues serine at position 213 (S213) and lysine at position 218 (K218), which are present in close proximity to the histidine-rich motif II of Mucor rouxii fatty acid Delta(6)-desaturase isoform II, were targeted for studying structure-function relationships using site-directed mutagenesis. The mutants were functionally characterized in a heterologous host, Saccharomyces cerevisiae. Substrate specificity and preference studies revealed that S213 and K218 are involved in substrate recognition. K218 plays a role in substrate preference by involvement in the binding of substrates, particularly C15-C18 monoene fatty acids. Modification of the M. rouxii Delta(6)-desaturase therefore has potential in specifically altering substrate utilization for production of desired fatty acids. |
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Keywords: | Δ6-Desaturase Mucor rouxii γ-Linolenic acid Histidine-rich motif Site-directed mutagenesis Substrate recognition |
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