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Plant Physiol, March 2000, Vol. 122, pp. 715-720
Characterization of the Brassica napus
Extraplastidial Linoleate Desaturase by Expression in
Saccharomyces cerevisiae1
Darwin W.
Reed,
Ulrike A.
Schäfer, and
Patrick S.
Covello*
National Research Council of Canada, Plant Biotechnology Institute,
110 Gymnasium Place, Saskatoon, Saskatchewan, Canada S7N 0W9
The substrate specificity and
regioselectivity of the Brassica napus extraplastidial
linoleate desaturase (FAD3) was investigated in vivo in
a heterologous expression system. A strain of the yeast Saccharomyces cerevisiae producing the plant enzyme was
constructed and cultured in media containing a variety of fatty acids.
The products of desaturation of these potential substrates were
determined by gas chromatographic and mass spectrometric analysis of
the yeast cultures. The results indicate that the enzyme has: (a)  -3, as opposed to  -15 or double-bond-related regioselectivity, (b) the ability to desaturate substrates in the 16 to 22 carbon range,
(c) a preference for substrates with -6 double bonds, but the
ability to desaturate substrates with -6 hydroxyl groups or -9 or
-5 double bonds, and (d) a relative insensitivity to double bonds
proximal to the carboxyl end of the substrate.
1
This is National Research Council of Canada
publication no. 42,628.
*
Corresponding author; e-mail patrick.covello{at}nrc.ca; fax
306-975-4839.
© 2000 American Society of Plant Physiologists
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