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-
aut
text
theses
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Hochschulschrift
gw
2015
monographic
XA-DE
2015
eng
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Online-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
2015
Druck-Ausgabe
(DE-627)843512199
Brosemann, Anne, 1986 -
urn:nbn:de:gbv:28-diss2015-0208-8
936054666
rakwb
DE-627
151214
843887001
20251224T201051.0
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