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 - 2000

Fingerprint

Borago
Fatty Acid Desaturases
Mutagenesis
Histidine
Glutamine
Consensus Sequence
Site-Directed Mutagenesis
Fusion reactions
Membranes
Enzymes
sphingolipid desaturase

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mutagenesis of the borage Δ6 fatty acid desaturase. / Sayanova, O.; Beaudoin, F.; Libisch, B.; Shewry, P.; Napier, J.

In: Biochemical Society Transactions, Vol. 28, No. 6, 2000, p. 636-638.

Research output: Contribution to journalArticle

Sayanova, O. ; Beaudoin, F. ; Libisch, B. ; Shewry, P. ; Napier, J. / Mutagenesis of the borage Δ6 fatty acid desaturase. In: Biochemical Society Transactions. 2000 ; Vol. 28, No. 6. pp. 636-638.
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