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A desaturase‐like protein from white spruce is a Δ 9 desaturase
Author(s) -
Marillia Elizabeth-France,
Giblin E.Michael,
Covello Patrick S,
Taylor David C
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03112-5
Subject(s) - biochemistry , biology , heterologous expression , complementary dna , yeast , enzyme , peptide sequence , fatty acid desaturase , microbiology and biotechnology , chemistry , gene , fatty acid , polyunsaturated fatty acid , recombinant dna
Gymnospermae seed lipids are characterized by a high degree of desaturation, most having a Δ 9 double bond. By degenerate polymerase chain reaction (PCR) we have isolated a white spruce ( Picea glauca ) cDNA clone that encodes an amino acid sequence sharing a high degree of homology with other putative plant acyl‐coenzyme A (CoA) Des9 desaturases. Both in vivo and in vitro expression studies in a Δ 9 desaturase‐deficient yeast strain demonstrated the desaturation functionality of the white spruce clone, and gas chromatography‐mass spectrometry (GC‐MS) analyses confirmed the regioselectivity of the encoded enzyme. This is the first report of the functional characterization of a plant membrane‐bound acyl‐CoA‐like protein Δ 9 desaturase by heterologous expression in yeast.