Mutagenesis of the borage Δ6 fatty acid desaturase

O. Sayanova, F. Beaudoin, B. Libisch, P. Shewry, J. Napier

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The consensus sequence of the third histidine box of a range of Δ5, Δ6, Δ8 and sphingolipid desaturases differs from that of the membrane-bound non-fusion Δ12 and Δ15 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 b5 fusion domain from the plant sphingolipid desaturase to substitute for the endogenous domain of the Δ6 desaturase.

Original languageEnglish
Pages (from-to)636-638
Number of pages3
JournalBiochemical Society transactions
Volume28
Issue number6
DOIs
Publication statusPublished - Jan 1 2000

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Keywords

  • Cyt b domain
  • Cytochrome b domain
  • Yeast expression
  • Δ-unsaturated fatty acid

ASJC Scopus subject areas

  • Biochemistry

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