Isolation of cDNAs and functional characterisation of two multi-product terpene synthase enzymes from sandalwood, Santalum album L.

Jones, Callum; Keeling, Christopher I.; Ghisalberti, Emilio L.; Barbour, Elizabeth L.; Plummer, Julie; Bohlmann, Jörg

doi:10.1016/j.abb.2008.05.008

Cited by 77 publications

(55 citation statements)

References 40 publications

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“…Co-occurrence patterns of the santalenes and bergamotene, as well as other olefins and bisabolol, indicated that multi-product TPS enzymes may be responsible for the production of several sandalwood oil components (2). Multiple product formation from terpene synthase (TPS) enzymes in S. album was recently confirmed by characterization of two TPSs, however these were not responsible for santalene biosynthesis (7). The commercially exploited sandalwoods possess unique chemical phenotypes (3), whereas others such as S. accuminatum and S. murrayanum, endemic to southwestern WA, produce little or no oil (8).…”

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confidence: 85%

Sandalwood Fragrance Biosynthesis Involves Sesquiterpene Synthases of Both the Terpene Synthase (TPS)-a and TPS-b Subfamilies, including Santalene Synthases

Jones

Moniodis²,

Zulak

et al. 2011

Journal of Biological Chemistry

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135

105

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Sandalwood oil is one of the worlds most highly prized fragrances. To identify the genes and encoded enzymes responsible for santalene biosynthesis, we cloned and characterized three orthologous terpene synthase (TPS) genes SaSSy, SauSSy, and SspiSSy from three divergent sandalwood species; Santalum album, S. austrocaledonicum, and S. spicatum, respectively. The encoded enzymes catalyze the formation of ␣-, ␤-, epi-␤-santalene, and ␣-exo-bergamotene from (E,E)-farnesyl diphosphate (E,E-FPP). Recombinant SaSSy was additionally tested with (Z,Z)-farnesyl diphosphate (Z,Z-FPP) and remarkably, found to produce a mixture of ␣-endo-bergamotene, ␣-santalene, (Z)-␤-farnesene, epi-␤-santalene, and ␤-santalene. Additional cDNAs that encode bisabolene/bisabolol synthases were also cloned and functionally characterized from these three species. Both the santalene synthases and the bisabolene/bisabolol synthases reside in the TPS-b phylogenetic clade, which is more commonly associated with angiosperm monoterpene synthases. An orthologous set of TPS-a synthases responsible for formation of macrocyclic and bicyclic sesquiterpenes were characterized. Strict functionality and limited sequence divergence in the santalene and bisabolene synthases are in contrast to the TPS-a synthases, suggesting these compounds have played a significant role in the evolution of the Santalum genus.

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confidence: 85%

Sandalwood Fragrance Biosynthesis Involves Sesquiterpene Synthases of Both the Terpene Synthase (TPS)-a and TPS-b Subfamilies, including Santalene Synthases

Jones

Moniodis²,

Zulak

et al. 2011

Journal of Biological Chemistry

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135

105

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“…Ref. 38). This study may resolve some of the discussion about single-or multi-product profiles of LAS-type diterpene synthases, a topic that was first raised with the variability of product identification of the grand fir AgAS enzyme (6,9).…”

Section: Discussionmentioning

confidence: 99%

The Primary Diterpene Synthase Products of Picea abies Levopimaradiene/Abietadiene Synthase (PaLAS) Are Epimers of a Thermally Unstable Diterpenol

Keeling

Madilao

Zerbe

et al. 2011

Journal of Biological Chemistry

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The levopimaradiene/abietadiene synthase from Norway spruce (Picea abies; PaLAS) has previously been reported to produce a mixture of four diterpene hydrocarbons when incubated with geranylgeranyl diphosphate as the substrate: levopimaradiene, abietadiene, neoabietadiene, and palustradiene. However, variability in the assay products observed by GC-MS of this and orthologous conifer diterpene synthases over the past 15 years suggested that these diterpenes may not be the initial enzyme assay products but are rather the products of dehydration of an unstable alcohol. We have identified epimers of the thermally unstable allylic tertiary alcohol 13-hydroxy-8(14)-abietene as the products of PaLAS. The identification of these compounds, not previously described in conifers, as the initial products of PaLAS has considerable implications for our understanding of the complexity of the biosynthetic pathway of the structurally diverse diterpene resin acids of conifer defense.

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“…Such a broad product spectrum is uncommon and in contrast to this, the majority (>80%) of sesquiterpene synthases form only one single product [3]. All sesquiterpene synthases transform the structurally relatively simple substrate E,E-farnesyl diphosphate (FDP, C 15 unit) into various sesquiterpenes including macrocyclic, bicyclic and tricyclic compounds [4].…”

Section: Introductionmentioning

confidence: 99%

Characterisation of a Recombinant Patchoulol Synthase Variant for Biocatalytic Production of Terpenes

Frister

Hartwig

Alemdar

et al. 2015

Appl Biochem Biotechnol

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The patchoulol synthase (PTS) is a multi-product sesquiterpene synthases which is the central enzyme for biosynthesis of patchouli essential oil in the patchouli plant. Sesquiterpene synthases catalyse the formation of various complex carbon backbones difficult to approach by organic synthesis. Here, we report the characterisation of a recombinant patchoulol synthase complementary DNA (cDNA) variant (PTS var. 1), exhibiting significant amino acid exchanges compared to the native PTS. The product spectrum using the natural substrate E,E-farnesyl diphosphate (FDP) as well as terpenoid products resulting from conversions employing alternative substrates was analysed by GC-MS. In respect to a potential use as a biocatalyst, important enzymatic parameters such as the optimal reaction conditions, kinetic behaviour and the product selectivity were studied as well. Adjusting the reaction conditions, an increased patchoulol ratio in the recombinant essential oil was achieved. Nevertheless, the ratio remained lower than in plant-derived patchouli oil. As alternative substrates, several prenyl diposphates were accepted and converted in numerous compounds by the PTS var. 1, revealing its great biocatalytic potential.

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Isolation of cDNAs and functional characterisation of two multi-product terpene synthase enzymes from sandalwood, Santalum album L.

Cited by 77 publications

References 40 publications

Sandalwood Fragrance Biosynthesis Involves Sesquiterpene Synthases of Both the Terpene Synthase (TPS)-a and TPS-b Subfamilies, including Santalene Synthases

Sandalwood Fragrance Biosynthesis Involves Sesquiterpene Synthases of Both the Terpene Synthase (TPS)-a and TPS-b Subfamilies, including Santalene Synthases

The Primary Diterpene Synthase Products of Picea abies Levopimaradiene/Abietadiene Synthase (PaLAS) Are Epimers of a Thermally Unstable Diterpenol

Characterisation of a Recombinant Patchoulol Synthase Variant for Biocatalytic Production of Terpenes

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