Complexes of bivalent cations with neryl and geranyl pyrophosphate: Their role in terpene biosynthesis

Chayet, L.; Rojas, María Cecilia; Cori, Osvaldo; Bunton, Clifford A.; McKenzie, D. C.

doi:10.1016/0045-2068(84)90014-2

Cited by 30 publications

(14 citation statements)

References 28 publications

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“…The divalent metal ion binds to the pyrophosphate moiety of the allylic cosubstrate, so as to neutralize/shield negative charges of the pyrophosphate moiety and to make it a better leaving group in the ionization step (Chayet et al, 1984;McGarvey and Croteau, 1995). Ionization of the allylic pyrophosphate (FPP) leads to formation of a chargestabilized allylic carbocation (Chayet et al, 1984;McCaskill and Croteau, 1997;McGarvey and Croteau, 1995) as an intermediate of sesquiterpene formation.…”

Section: Discussionmentioning

confidence: 99%

Sesquiterpene α-Farnesene Synthase: Partial Purification, Characterization, and Activity in Relation to Superficial Scald Development in Apples

Rupasinghe¹,

Paliyath²,

Murr³

2000

jashs

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To decipher the relation between α-farnesene metabolism and the development of superficial scald in apples, trans,trans-α-farnesene synthase, the enzyme that catalyzes the conversion of farnesyl pyrophosphate to α-farnesene, was partially purified from skin tissue of `Delicious' apples (Malus ×domestica Borkh.) and characterized. Total and specific activities of the enzyme were higher in the cytosolic fraction than in membrane fractions. α-Farnesene synthase was purified 70-fold from the cytosolic fraction by ion exchange chromatography and gel permeation, and the native molecular weight was estimated to be 108,000. The enzyme had optimal activity at a pH of 5.6 and absolutely required a divalent metal ion such as Mg2+ or Mn2+ for activity. It exhibited allosteric kinetics, S(0.5) for farnesyl pyrophosphate being 84±18 μmol·L-1, and a Hill coefficient (nH) of 2.9, indicating the number of subunits to be two or three. Enzyme activity was highest between 10 and 20 °C, while 50% of the maximal activity was retained at 0 °C. In vivo α-farnesene synthase activity was minimal at harvest, then increased rapidly during 16 weeks storage in air at 0 °C, and decreased during further storage. Activity of α-farnesene synthase, α-farnesene content, and conjugated triene alcohol (the putative scald-causing oxidation product of α-farnesene) content in skin tissue were not correlated to the inherent nature of scald susceptibility or resistance in 11 apple cultivars tested.

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Section: Discussionmentioning

confidence: 99%

Sesquiterpene α-Farnesene Synthase: Partial Purification, Characterization, and Activity in Relation to Superficial Scald Development in Apples

Rupasinghe¹,

Paliyath²,

Murr³

2000

jashs

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“…Terpene synthases are in general stimulated by the presence of divalent cations such as Mg 2+ or Mn 2+ , as they are required for the stabilization of the negative pyrophosphate moiety of the isoprenyl substrate [3,24]. The effect of Mg 2+ and Mn 2+ on PSY activity in partially purified enzyme preparations was investigated.…”

Section: Characterization Of Psymentioning

confidence: 99%

Modulation of carotenoid biosynthesis during tomato fruit ripening through phytochrome regulation of phytoene synthase activity

Schofield

Paliyath

2005

Plant Physiology and Biochemistry

100

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“…3a & b). The enhanced production of minor products could be due to the geometric configuration of NPP, which may be a better substrate for their synthesis through direct cyclization (Chayet et al 1984). The ability of TPSs (including LiCINS) to produce multiple products may have resulted from incomplete evolution of the active sites of the ancestral protein to achieve precision in its catalytic activity (Christianson 2006).…”

Section: Recombinant Production and Functional Assaymentioning

confidence: 99%

Cloning, functional characterization and genomic organization of 1,8-cineole synthases from Lavandula

et al. 2012

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Several members of the genus Lavandula produce valuable essential oils (EOs) that are primarily constituted of the low molecular weight isoprenoids, particularly monoterpenes. We isolated over 8,000 ESTs from the glandular trichomes of L. x intermedia flowers (where bulk of the EO is synthesized) to facilitate the discovery of genes that control the biosynthesis of EO constituents. The expression profile of these ESTs in L. x intermedia and its parents L. angustifolia and L. latifolia was established using microarrays. The resulting data highlighted a differentially expressed, previously uncharacterized cDNA with strong homology to known 1,8-cineole synthase (CINS) genes. The ORF, excluding the transit peptide, of this cDNA was expressed in E. coli, purified by Ni-NTA agarose affinity chromatography and functionally characterized in vitro. The ca. 63 kDa bacterially produced recombinant protein, designated L. x intermedia CINS (LiCINS), converted geranyl diphosphate (the linear monoterpene precursor) primarily to 1,8-cineole with K ( m ) and k ( cat ) values of 5.75 μM and 8.8 × 10(-3) s(-1), respectively. The genomic DNA of CINS in the studied Lavandula species had identical exon-intron architecture and coding sequences, except for a single polymorphic nucleotide in the L. angustifolia ortholog which did not alter protein function. Additional nucleotide variations restricted to L. angustifolia introns were also observed, suggesting that LiCINS was most likely inherited from L. latifolia. The LiCINS mRNA levels paralleled the 1,8-cineole content in mature flowers of the three lavender species, and in developmental stages of L. x intermedia inflorescence indicating that the production of 1,8 cineole in Lavandula is most likely controlled through transcriptional regulation of LiCINS.

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Complexes of bivalent cations with neryl and geranyl pyrophosphate: Their role in terpene biosynthesis

Cited by 30 publications

References 28 publications

Sesquiterpene α-Farnesene Synthase: Partial Purification, Characterization, and Activity in Relation to Superficial Scald Development in Apples

Sesquiterpene α-Farnesene Synthase: Partial Purification, Characterization, and Activity in Relation to Superficial Scald Development in Apples

Modulation of carotenoid biosynthesis during tomato fruit ripening through phytochrome regulation of phytoene synthase activity

Cloning, functional characterization and genomic organization of 1,8-cineole synthases from Lavandula

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