Isolation and characterization of a calendic acid producing (8,11)-linoleoyl desaturase.
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.
Fritsche
K
K
Leibniz Institut für Pflanzenbiochemie, Weinberg, Halle, Germany.
Hornung
E
E
Peitzsch
N
N
Renz
A
A
Feussner
I
I
D000595:Amino Acid Sequence; D020838:Calendula / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D044943:Fatty Acid Desaturases / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification*; D005227:Fatty Acids / Q000032:analysis*; D050602:Linoleoyl-CoA Desaturase; D008969:Molecular Sequence Data; D010802:Phylogeny; D010946:Plants, Medicinal; D016133:Polymerase Chain Reaction; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D005227:Fatty Acids; D044943:Fatty Acid Desaturases; D050602:Linoleoyl-CoA Desaturase