Targeted mutagenesis of a fatty acid Δ6-desaturase from Mucor rouxii: Role of amino acid residues adjacent to histidine-rich motif II

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 Δ6-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 Δ6-desaturase therefore has potential in specifically altering substrate utilization for production of desired fatty acids.