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Linalool synthase

The Arabidopsis GES protein shares 40% sequence identity with two characterized linalool synthases from Clarkia breweri and Clarkia concinna [65], which together belong to the TPS-f family (Fig. 11.4). Linalool synthases catalyze a reaction analogous to that of GES by converting the 10-carbon substrate GPP into... [Pg.167]

Dudareva N, Cseke L, Blanc VM, Pichersky E (1996) Evolution of floral scent in Clarkia Novel patterns of S-linalool synthase gene expression in the C. breweri flower. Plant Cell 8 1137-1148... [Pg.176]

Figure 10.1. The gene from Clarkia breweri coding for (S)-linalool synthase (LIS) was added to three different piant species (tomato, petunia and carnation) and each species produced the expected product, S-iinaiooi. However, the existing NP metabolic flexibility in each species aiiowed the novei substance, S-iinaiooi, to be converted to other substances, those substances being different in each species due to the differences in NP metabolism in each plant. ... Figure 10.1. The gene from Clarkia breweri coding for (S)-linalool synthase (LIS) was added to three different piant species (tomato, petunia and carnation) and each species produced the expected product, S-iinaiooi. However, the existing NP metabolic flexibility in each species aiiowed the novei substance, S-iinaiooi, to be converted to other substances, those substances being different in each species due to the differences in NP metabolism in each plant. ...
Not all attempts at metabolic engineering deliver the expected results. For example, Liicker et al. [11] transformed petunia (Petunia hybrida) with the (S)-linalool synthase (LIS) gene from Clarkia breweri (Scheme 26.1), but despite... [Pg.617]

DUDAREVA, N., CSEKE L., BLANC, V.M., PICHERSKY, E., Evolution of floral scent in Clarkiar. Novel Patterns of S-linalool synthase gene expression in Clarkia breweri flowers., Plant Cell, 1996,8,1837-1848. [Pg.199]

Our recent research suggests organ-, tissue-, and cell-specific localization of constitutive and induced terpenoid defense pathways in conifers. For example, linalool synthase (PaTPS-Lin) seems to be preferentially expressed in needles of Norway spruce and Sitka spruce with little or no expression in sterns. ft is also likely that expression of PaTPS-Lin in spruce needles is not associated with resin ducts but could reside in other cells involved with induced terpenoid emission. In contrast, we can speculate that most other mono-TPS and di-TPS are associated with epithelial cells of constitutive and induced resin ducts. The possible localization of conifer sesqui-TPS is difficult to predict. Furthermore, the exact spatial and temporal patterns of terpenoid pathway gene expression associated with traumatic resin duct development in the cambium zone and outer xylem remain to be studied at the tissue and cell level. In situ hybridization and immuno-localization of TPS will address these open questions. These methods have worked well in identifying cell type specific gene and protein expression of alkaloid formation in opium poppy Papaver somniferum) As the biochemistry of induced terpene defenses and the development of traumatic resin ducts have been well described in spruce, this system is ideal for future studies of tissue- and cell-specific localization of transcripts and proteins associated with oleoresin defense and induced volatile emissions in conifers. In addition, the advent of laser dissection microscopy techniques presents a fascinating means by which to further address RNA and protein analysis in a tissue-and cell-specific manner. These techniques, when applied to the cambium zone, xylem mother cells, and the epithelial cells that surround traumatic resin ducts, and will allow a temporal and spatial analysis of cellular functions occurring in the traumatic resin response. [Pg.48]

Pichersky, E., Lewinsohn, E., and Croteau, R., Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri,Arch Biochem. Biophys., 316, 803, 1995. [Pg.309]

Really, there are today already several examples for producing the same molecule as active com pound by different enzymes and thus likely on the base of different genetic determination. Linalool synthase from Clarkia brewed has different constitution than linalool synthase from Arabidopsis plants (Dudareva et al., 2006) and only 41% identity to the same enzyme fromM. citrata (Crowell et al., 2002). The enzyme from M. citrata is, however, much more close to other enzymes from the mint (Lamiaceae) family with 62%-72% identity. [Pg.114]

Liicker J, Bouwmeester HJ, Schwab W, Blaas J, van der Plas LHW, Verhoeven HA (2001) Expression of Clarkia S-linalool synthase in transgenic petunia plants results in the accumulation of S-linalyl-P-D-glucopyranoside. Plant 27 315-324... [Pg.2685]

Schie CCN, van Haring MA, Schuurink, RC (2007) Tomato linalool synthase is induced in trichomes by jasmonic acid. Plant Mol Biol 64 251-263 Schindek R, Hilker M (1996) Influence of larvae of Gastrophysa viridula on the distribution of con-... [Pg.345]

Lavy, M., et al. (2002) Linalool and linalool oxide production in transgenic carnation flowers expressing the Clarkia breweri linalool synthase gene. Mol. Breed. 9, 103-111... [Pg.433]

Pichersky E (1998) Use of linalool synthase in genetic engineering of scent production. US patent No 5849526A... [Pg.300]


See other pages where Linalool synthase is mentioned: [Pg.167]    [Pg.167]    [Pg.167]    [Pg.168]    [Pg.170]    [Pg.210]    [Pg.618]    [Pg.2144]    [Pg.318]    [Pg.318]    [Pg.36]    [Pg.45]    [Pg.119]    [Pg.406]    [Pg.418]    [Pg.420]    [Pg.449]    [Pg.450]   
See also in sourсe #XX -- [ Pg.36 , Pg.45 , Pg.48 ]




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