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Isolation and characterization of a calendic acid producing (8,11)‐linoleoyl desaturase 1
Author(s) -
Fritsche Kathrin,
Hornung Ellen,
Peitzsch Nicola,
Renz Andreas,
Feussner Ivo
Publication year - 1999
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(99)01541-0
Subject(s) - complementary dna , biochemistry , open reading frame , heterologous expression , amino acid , saccharomyces cerevisiae , peptide sequence , enzyme , stearoyl coa desaturase , cloning (programming) , biology , biosynthesis , fatty acid desaturase , gene , fatty acid , microbiology and biotechnology , chemistry , gene expression , recombinant dna , polyunsaturated fatty acid , computer science , programming language
For the biosynthesis of calendic acid a (8,11)‐linoleoyl desaturase activity has been proposed. To isolate this desaturase, PCR‐based cloning was used. The open reading frame of the isolated full‐length cDNA is a 1131 bp sequence encoding a protein of 377 amino acids. For functional identification the cDNA was expressed in Saccharomyces cerevisiae , and formation of calendic acid was analyzed by RP‐HPLC. The expression of the heterologous enzyme resulted in a significant amount of calendic acid presumably esterified within phospholipids. The results presented here identify a gene encoding a new type of (1,4)‐acyl lipid desaturase.