Biochemical analysis of the α-terpineol/1,8-cineole cyclization reaction of the cineole synthase of Nicotiana suaveolens Biochemical analysis of the [alpha]-terpineol/1,8-cineole cyclization reaction of the cineole synthase of Nicotiana suaveolens Brosemann, Anne , 1986- Text theses Text Hochschulschrift 2015 2015 eng electronic resourceremoteComputermedienOnline-Ressourcetext/htmlapplication/pdfOnline-Ressource Illustrationen (farbig), Diagramme 19 mutants of the cineole synthase of N. suaveolens were generated by site-directed mutagenesis in order to substitute the amino acids of the cineole synthase with amino acids of the equivalent position of the terpineol synthase of N. langsdorfii. The mutant enzyme F266S carrying a phenylalanine replacement by serine showed an inverted product spectrum compared to the wild type enzyme. Terpineol was the major compound in the product profile of the mutant F266S. It is hypothesized that the synthesis of cineole proceeds independent of terpineol and via α-terpinyl hydronium ion (Wise et al. 2002). vorgelegt von Anne Brosemann Rostock, Univ., Mathematisch-Naturwiss. Fak., Diss., 2015 572.54523952 547.71 570 540 35.70 42.13 42.41 http://rosdok.uni-rostock.de/resolve?urn=urn:nbn:de:gbv:28-diss2015-0208-8 http://rosdok.uni-rostock.de/resolve?urn=urn:nbn:de:gbv:28-diss2015-0208-8&pdf http://nbn-resolving.de/urn:nbn:de:gbv:28-diss2015-0208-8 Biochemical analysis of the α-terpineol/1,8-cineole cyclization reaction of the cineole synthase of Nicotiana suaveolens--(DE-627)843512199 urn:nbn:de:gbv:28-diss2015-0208-8 oclc: 936054666 ppn: (DE-627)843887001