Cloning and functional characterization of three terpene synthases from lavender (Lavandula angustifolia).
The essential oil of lavender (Lavandula angustifolia) is mainly composed of mono- and sesquiterpenes. Using a homology-based PCR strategy, two monoterpene synthases (LaLIMS and LaLINS) and one sesquiterpene synthase (LaBERS) were cloned from lavender leaves and flowers. LaLIMS catalyzed the formation of (R)-(+)-limonene, terpinolene, (1R,5S)-(+)-camphene, (1R,5R)-(+)-alpha-pinene, beta-myrcene and traces of alpha-phellandrene. The proportions of these products changed significantly when Mn(2+) was supplied as the cofactor instead of Mg(2+). The second enzyme LaLINS produced exclusively (R)-(-)-linalool, the main component of lavender essential oil. LaBERS transformed farnesyl diphosphate and represents the first reported trans-alpha-bergamotene synthase. It accepted geranyl diphosphate with higher affinity than farnesyl diphosphate and also produced monoterpenes, albeit at low rates. LaBERS is probably derived from a parental monoterpene synthase by the loss of the plastidial signal peptide and by broadening its substrate acceptance spectrum. The identification and description of the first terpene synthases from L. angustifolia forms the basis for the biotechnological modification of essential oil composition in lavender.
Biomolecular Food Technology, Technical University Munich, Lise-Meitner-Str. 34, 85354 Freising, Germany.
Christian
C
Landmann
Barbara
B
Fink
Maria
M
Festner
Márta
M
Dregus
Karl-Heinz
KH
Engel
Wilfried
W
Schwab
D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000145:classification* / Q000235:genetics; D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004789:Enzyme Activation; D004795:Enzyme Stability; D027523:Lavandula / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry; D013379:Substrate Specificity
D011994:Recombinant Proteins; D019883:Alkyl and Aryl Transferases; C108877:terpene synthase