Chimeras of delta6-fatty acid and delta8-sphingolipid desaturases

A - Papers appearing in refereed journals

Libisch, B., Michaelson, L. V., Lewis, M. J., Shewry, P. R. and Napier, J. A. 2000. Chimeras of delta6-fatty acid and delta8-sphingolipid desaturases. Biochemical and Biophysical Research Communications. 279 (3), pp. 779-785.

AuthorsLibisch, B., Michaelson, L. V., Lewis, M. J., Shewry, P. R. and Napier, J. A.
Abstract

The Borago officinalis Delta6 fatty acid desaturase (Boofd6) shares 58% identity in its amino acid sequence with Boofd8, a Delta8 sphingolipid desaturase from the same plant species. In order to localise the distinct catalytic properties of Boofd6 and Boofd8 to individual regions within them, a set of chimeras of these two enzymes were constructed and expressed in yeast. Chimera 2 is different from the other chimeras and Boofd6 in that it did not have any detectable desaturase activity on 18 carbon fatty acids. However, it desaturated C16 palmitoleic and C14 myristoleic acid, and the conversion rate for the later one was more than three times higher than that of Boofd6. These results suggest that the predicted membrane helices 1 and 2 of Boofd6 are involved in forming the substrate-binding site. This site appears to place constraints on the chain length of fatty acid substrates, which is similar to hydrophobic substrate binding pockets.

KeywordsDelta (6) desaturase; sphingolipid; chimera; gamma-linolenic-acid; substrate-binding site; yeast
Year of Publication2000
JournalBiochemical and Biophysical Research Communications
Journal citation279 (3), pp. 779-785
Digital Object Identifier (DOI)doi:10.1006/bbrc.2000.4023
PubMed ID11162428
Open accessPublished as non-open access
Funder project or code415
Isolation of DNAs for novel fatty acid desaturase enzymes and their use to manipulate fatty acid and triglycerol composition in transgenic plants
FunderBiotechnology and Biological Sciences Research Council
Output statusPublished
Publication dates
Print29 Dec 2000
Online25 May 2002
Copyright licensePublisher copyright
PublisherAcademic Press Inc Elsevier Science
ISSN0006-291X

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