Targeted mutagenesis of a fatty acid Delta super(6)-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 Delta super(6)-desaturase isoform II, were targeted for studying structure-function relationships using site-directe...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-01, Vol.339 (4), p.1029-1034
Main Authors: Na-Ranong, S, Laoteng, K, Kittakoop, P, Tanticharoen, M, Cheevadhanarak, S
Format: Article
Language:English
Subjects:
Mucor rouxii
Saccharomyces cerevisiae
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Summary: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 super(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 super(6)-desaturase therefore has potential in specifically altering substrate utilization for production of desired fatty acids.
ISSN:0006-291X
DOI:10.1016/j.bbrc.2005.11.115