Mutagenesis of the borage Δ6 fatty acid desaturase. (December 2000)

• Record Type: Journal Article
• Authors: Sayanova, O.; Beaudoin, F.; Libisch, B.; Shewry, P.; Napier, J.
• Is Part Of: Biochemical Society transactions. Volume 28:Number 6(2000)
• Page Start: 636
• Page End: 638
• Publication Date: 2000-12
• Subjects: cyt bs domain -- cytochrome bs domain -- Δ6-unsaturated fatty acid -- yeast expression; cyt, cytochrome; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0280636
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : The consensus sequence of the third histidine box of a range of Δ 5, Δ 6, Δ 8 and sphingolipid desaturases differs from that of the membrane-bound non-fusion Δ 12 and Δ 15 desaturases in the presence of glutamine instead of histidine. We have used site-directed mutagenesis to determine the importance of glutamine and other residues of the third histidine box and created a chimaeric enzyme to determine the ability of the Cyt b 5 fusion domain from the plant sphingolipid desaturase to substitute for the endogenous domain of the Δ 6 desaturase.