Purification and Characterization of Geranyl Diphosphate Synthase from Vitis vinifera L. cv Muscat de Frontignan Cell Cultures

Clastre, Marc; Bantignies, Brigitte; Féron, Gilles; Soler, E.; Ambid, Christian

doi:10.1104/pp.102.1.205

Cited by 43 publications

(17 citation statements)

References 6 publications

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“…Kinetic evaluation of the recombinant, truncated version of GPPS (tetrameric form) provided an apparent K M (DMAPP) value of 54 M and a K M (MgCl 2 ) value of 2.1 mM, which are within the range of values previously reported for partially purified, native GPP synthases from other sources; however, the apparent K M (IPP) value of 26 M is 2-4 times higher than values reported for other prenyltransferases of this type (Table I) (21,(37)(38)(39). GPPS was unable to utilize GPP or FPP as the allylic cosubstrate with IPP, consistent with the observed chain length specificity of this enzyme.…”

Section: Resultsmentioning

confidence: 42%

Interaction with the Small Subunit of Geranyl Diphosphate Synthase Modifies the Chain Length Specificity of Geranylgeranyl Diphosphate Synthase to Produce Geranyl Diphosphate

Burke

Croteau

2002

Journal of Biological Chemistry

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Geranyl diphosphate synthase belongs to a subgroup of prenyltransferases, including farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase, that catalyzes the specific formation, from C 5 units, of the respective C 10 , C 15 , and C 20 precursors of monoterpenes, sesquiterpenes, and diterpenes. Unlike farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase, which are homodimers, geranyl diphosphate synthase from Mentha is a heterotetramer in which the large subunit shares functional motifs and a high level of amino acid sequence identity (56 -75%) with geranylgeranyl diphosphate synthases of plant origin. The small subunit, however, shares little sequence identity with other isoprenyl diphosphate synthases; yet it is absolutely required for geranyl diphosphate synthase catalysis. Coexpression in Escherichia coli of the Mentha geranyl diphosphate synthase small subunit with the phylogenetically distant geranylgeranyl diphosphate synthases from Taxus canadensis and Abies grandis yielded a functional hybrid heterodimer that generated geranyl diphosphate as product in each case. These results indicate that the geranyl diphosphate synthase small subunit is capable of modifying the chain length specificity of geranylgeranyl diphosphate synthase (but not, apparently, farnesyl diphosphate synthase) to favor the production of C 10 chains. Comparison of the kinetic behavior of the parent prenyltransferases with that of the hybrid enzyme revealed that the hybrid possesses characteristics of both geranyl diphosphate synthase and geranylgeranyl diphosphate synthase.A subgroup of isoprenyl diphosphate synthases, referred to as the "short-chain prenyltransferases," consists of geranyl diphosphate (GPP 1 ; C 10 ) synthase, farnesyl diphosphate (FPP; C 15 ) synthase, and geranylgeranyl diphosphate (GGPP; C 20 ) synthase. These enzymes provide the acyclic branch point intermediates for the biosynthesis of numerous terpenoids, including monoterpenes, sesquiterpenes, diterpenes, triterpenes, tetraterpenes, and polyterpenes such as natural rubber. GGPP synthase and FPP synthase occur nearly ubiquitously in plants, animals, and bacteria (1). GPP synthase appears to be of much more limited distribution in nature, having been identified most frequently in essential oil (monoterpene)-producing plants (2). Most isoprenyl diphosphate synthases, including the short-chain prenyltransferases, catalyze the divalent metal iondependent 1Ј-4 condensation of isopentenyl diphosphate (IPP) with an allylic prenyl diphosphate cosubstrate (3), and they are distinguished by the specific chain length and double bond geometry at C2-C3 of the prenyl diphosphate product generated (Fig. 1). Thus, GPP synthase catalyzes a single condensation of IPP with dimethylallyl diphosphate (DMAPP) to form, specifically, GPP (C 10 ). FPP synthase and GGPP synthase catalyze sequential condensations of IPP with an allylic primer (i.e. DMAPP, GPP, or FPP, as appropriate) to form the respective C 15 and C 20 elongation products. Reaction paramet...

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Section: Resultsmentioning

confidence: 42%

Interaction with the Small Subunit of Geranyl Diphosphate Synthase Modifies the Chain Length Specificity of Geranylgeranyl Diphosphate Synthase to Produce Geranyl Diphosphate

Burke

Croteau

2002

Journal of Biological Chemistry

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“…Unlike the ubiquitous prenyltransferases, FPP synthase and GGPP synthase (2), GPP synthase is largely restricted to plant species that produce abundant quantities of monoterpenes (7)(8)(9)(10)(11)(12). The epidermal oil glands are the exclusive site of monoterpene biosynthesis in mint (Mentha) species (17).…”

Section: Resultsmentioning

confidence: 99%

“…Thus far, GPP synthase is known only at the enzyme level, having been isolated from several plant sources (7)(8)(9)(10) where it appears to participate primarily in the plastidial biosynthesis of monoterpenes (11,12) by supplying the essential precursor of this family of natural products (13,14). The reported properties of GPP synthase vary somewhat; however, in mechanism and many reaction parameters, the GPP synthase resembles both FPP synthase and GGPP synthase (2,3,13).…”

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confidence: 99%

Geranyl diphosphate synthase: Cloning, expression, and characterization of this prenyltransferase as a heterodimer

Burke

Wildung

Croteau

1999

Proc. Natl. Acad. Sci. U.S.A.

193

145

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Geranyl diphosphate synthase, which catalyzes the condensation of dimethylallyl diphosphate and isopentenyl diphosphate to geranyl diphosphate, the key precursor of monoterpene biosynthesis, was purified from isolated oil glands of spearmint. Peptide fragments generated from the pure proteins of 28 and 37 kDa revealed amino acid sequences that matched two cDNA clones obtained by random screening of a peppermint-oil gland cDNA library. The deduced sequences of both proteins showed some similarity to existing prenyltransferases, and both contained a plastid-targeting sequence. Expression of each cDNA individually yielded no detectable prenyltransferase activity; however, coexpression of the two together produced functional geranyl diphosphate synthase. Antibodies raised against each protein were used to demonstrate that both subunits were required to produce catalytically active native and recombinant enzymes, thus confirming that geranyl diphosphate synthase is a heterodimer. monoterpene biosynthesis ͉ isoprenoid biosynthesis

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“…Vitis vinifera Clastre et al (1993) 16. ondary compounds. Only carbon that has accumulated in excess of growth requirements can be allocated to carbonbased defence strategies.…”

Section: 5mentioning

confidence: 99%

Strong correlation between isoprene emission and gross photosynthetic capacity during leaf phenology of the tropical tree species Hymenaea courbaril with fundamental changes in volatile organic compounds emission composition during early leaf development

Kühn

Rottenberger

Biesenthal

et al. 2004

Plant Cell & Environment

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Changes of the volatile organic compounds (VOC) emission capacity and composition of different developmental stages of the tropical tree species Hymenaea courbaril were investigated under field conditions at a remote Amazonian rainforest site. The basal emission capacity of isoprene changed considerably over the course of leaf development, from young to mature and to senescent leaves, ultimately spanning a wide range of observed isoprene basal emission capacities from 0.7 to 111.5 m m m m g C g ---during the course of the year. By adjusting the standard emission factors for individual days, the diel courses of instantaneous isoprene emission rates could nevertheless adequately be modelled by a current isoprene algorithm. The results demonstrate the inadequacy of using one single standard emission factor to represent the VOC emission capacity of tropical vegetation for an entire seasonal cycle. A strong linear correlation between the isoprene emission capacity and the gross photosynthetic capacity (GP max ) covering all developmental stages and seasons was observed. The present results provide evidence that leaf photosynthetic properties may confer a valuable basis to model the seasonal variation of isoprenoid emission capacity; especially in tropical regions where the environmental conditions vary less than in temperate regions. In addition to induction and variability of isoprene emission during early leaf development, considerable amounts of monoterpenes were emitted in a light-dependent manner exclusively in the period between bud break and leaf maturity. The fundamental change in emission composition during this stage as a consequence of resource availability ( supply side control ) or as a plant's response to the higher defence demand of young emerging leaves ( demand-side control ) is discussed. The finding of a temporary emergence of monoterpene emission may be of general interest in understanding both the ecological functions of isoprenoid production and the regulatory processes involved.

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Purification and Characterization of Geranyl Diphosphate Synthase from Vitis vinifera L. cv Muscat de Frontignan Cell Cultures

Cited by 43 publications

References 6 publications

Interaction with the Small Subunit of Geranyl Diphosphate Synthase Modifies the Chain Length Specificity of Geranylgeranyl Diphosphate Synthase to Produce Geranyl Diphosphate

Interaction with the Small Subunit of Geranyl Diphosphate Synthase Modifies the Chain Length Specificity of Geranylgeranyl Diphosphate Synthase to Produce Geranyl Diphosphate

Geranyl diphosphate synthase: Cloning, expression, and characterization of this prenyltransferase as a heterodimer

Strong correlation between isoprene emission and gross photosynthetic capacity during leaf phenology of the tropical tree species Hymenaea courbaril with fundamental changes in volatile organic compounds emission composition during early leaf development

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