Biochemical analysis of the alpha-terpineol/1,8-cineole cyclization reaction of the cineole synthase of Nicotiana suaveolens

Anne Brosemann

doi:10.18453/rosdok_id00001658

Anne Brosemann

Biochemical analysis of the alpha-terpineol/1,8-cineole cyclization reaction of the cineole synthase of Nicotiana suaveolens

Universität Rostock, 2015

https://doi.org/10.18453/rosdok_id00001658

Abstract: 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).

Dissertation Freier Zugang

Titel:

Biochemical analysis of the alpha-terpineol/1,8-cineole cyclization reaction of the cineole synthase of Nicotiana suaveolens

Weitere Titel:

Biochemische Analyse der alpha-Terpinol/1,8-Cineol Zyklisierungsreaktion der Cineolsynthase aus Nicotiana suaveolens [übersetzt]

Beteiligte Personen:

Anne Brosemann[VerfasserIn]
	1080058109
Birgit Piechulla , Porf. Dr.[AkademischeR BetreuerIn]
	131807838
	Universität Rostock, Institut für Biowissenschaften, Abteilung Biochemie
Jörg Degenhardt , Prof. Dr.[AkademischeR BetreuerIn]
	Martin-Luther-Universität Halle-Wittenberg, Arbeitsgruppe Pharmazeutische Biotechnologie

Beteiligte Körperschaften:

Universität Rostock, Mathematisch-Naturwissenschaftliche Fakultät[Grad-verleihende Institution]
	2147083-2

Zusammenfassung:

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). [Englisch]

Dokumenttyp:

Dissertation

Einrichtung:

Mathematisch-Naturwissenschaftliche Fakultät

Sprache:

Englisch

Sachgruppe der DNB:

570 Biowissenschaften, Biologie

Veröffentlichung /
Entstehung:

Rostock

Rostock: Universität Rostock

2015