Isoprene Synthase Genes Form a Monophyletic Clade of Acyclic Terpene Synthases in the TPS-B Terpene Synthase Family

Sharkey, Thomas D.; Gray, Dennis W.; Pell, Heather K.; Breneman, Steven R.; Topper, Lauren A.

doi:10.1111/evo.12013

Cited by 91 publications

(157 citation statements)

References 92 publications

(119 reference statements)

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“…Non-linear regression revealed that the Km values of IspSs from P. alba, F. septica, and C. equisetifolia were 15.9, 3.4, and 0.3 mM, respectively. The Km value of 0.3 mM for IspS from C. equisetifolia was roughly comparable to the lowest concentration of 0.2 mM ever known and reported for IspS from E. globulus (Sharkey et al 2013). The high affinity of IspS from C. equisetifolia with substrate DMAPP prompted the authors to examine its activity on IPP and GPP.…”

Section: Resultssupporting

confidence: 66%

“…7a), making the shallow active site to only accept DMAPP (Gray et al 2011;Koksal et al 2010). Furthermore, it has been considered that amino acids unique to IspS "isoprene score" consisted of four canonical amino acid residues homologous to F338, S445, F485, and N505 of P. alba IspS (Sharkey et al 2013). In this context, the "isoprene score" is 4 for IspS from F. septica and F. virgata, and 3 for C. equisetifolia IspS (Fig.…”

Section: Discussionmentioning

confidence: 99%

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Molecular cloning and biochemical characterization of isoprene synthases from the tropical trees Ficus virgata, Ficus septica, and Casuarina equisetifolia

et al. 2015

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Three isoprene synthase (IspS) cDNA clones have been isolated from tropical trees (Ficus septica, F. virgata, and Casuarina equisetifolia), and their enzyme properties have been compared with those of Populus alba IspS. Phylogenetic analysis of the deduced amino acid sequences with known monoterpene synthase resolved IspS from F. septica and F. virgata and other IspSs in a clade together with TPS-b clade I, whereas IspS from C. equisetifolia was within another clade, sister to TPS-b clade II. The optimum reaction temperature was 40 °C for the IspSs isolated from the tropical trees, and 45 °C for P. alba IspS. The optimum pH of the IspSs from the tropical trees peaked between pH 8 and pH10 contrasting with the rather broad optimum pH (7.5-10.5) of P. alba IspS. IspSs from F. septica and F. virgata were activated solely by Mg(2+), whereas IspS from C. equisetifolia was dependent more on Mn(2+) than on Mg(2+). Michaelis constant (Km) values of IspSs from tropical trees were lower than that of P. alba IspS. Analysis of inter fragment interaction energy of IspS-substrate complex model and crystal structure of bornyl diphosphate synthase (1N20) found that the coordination geometry of amino acids with higher attraction force is similar at the active site of C. equisetifolia IspS and bornyl diphosphate synthase. These observations suggest the occurrence of another group of IspSs in TPS-b subfamily and extend the knowledge on biochemical regulatory mechanism of isoprene emission from tropical trees.

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Section: Resultssupporting

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Molecular cloning and biochemical characterization of isoprene synthases from the tropical trees Ficus virgata, Ficus septica, and Casuarina equisetifolia

et al. 2015

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“…This work was done with eucalyptus, and the enzyme kinetics of eucalyptus isoprene synthase has recently been published (56). Eucalyptus isoprene synthase has a K m(DMADP) of 0.16 mM, k cat of 0.195 s Ϫ1 , and substrate inhibition (K is ) of 0.9 mM.…”

Section: Discussionmentioning

confidence: 99%

Feedback Inhibition of Deoxy-d-xylulose-5-phosphate Synthase Regulates the Methylerythritol 4-Phosphate Pathway

Banerjee

et al. 2013

Journal of Biological Chemistry

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156

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Background:The methylerythritol phosphate (MEP) pathway is required for the biosynthesis of plastid-derived isoprenoids from plants. Results: Deoxyxylulose-5-phosphate synthase (DXS) was cloned from Populus trichocarpa, and metabolic regulation was tested. Conclusion: Both isopentenyl diphosphate and dimethylallyl diphosphate inhibit DXS by competing with thiamine pyrophosphate. Significance: Prediction of isoprene emission from trees and bioengineering of MEP pathway will be aided by these results.

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“…Isoprene-emitting species constitute an exciting model system where a very large DXP/MEP pathway flux goes to isoprene synthesis under physiological conditions (Li and Sharkey, 2013b;Sharkey et al, 2013). In isoprene-emitting species, there is a concomitant use of the primary substrate DMADP between the plastidic synthesis of isoprene and isoprenoids with a larger molecular size, such as phytol residue of chlorophyll (C20) and carotenoids (C40; Ghirardo et al, 2014;Rasulov et al, 2014), and different from nonemitting species, isoprene emitters seem to support a much larger pool of DMADP without the onset of feedback inhibition Wright et al, 2014).…”

mentioning

confidence: 99%

Bisphosphonate Inhibitors Reveal a Large Elasticity of Plastidic Isoprenoid Synthesis Pathway in Isoprene-Emitting Hybrid Aspen

et al. 2015

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Recently, a feedback inhibition of the chloroplastic 1-deoxy-D-xylulose 5-phosphate (DXP)/2-C-methyl-D-erythritol 4-phosphate (MEP) pathway of isoprenoid synthesis by end products dimethylallyl diphosphate (DMADP) and isopentenyl diphosphate (IDP) was postulated, but the extent to which DMADP and IDP can build up is not known. We used bisphosphonate inhibitors, alendronate and zoledronate, that inhibit the consumption of DMADP and IDP by prenyltransferases to gain insight into the extent of end product accumulation and possible feedback inhibition in isoprene-emitting hybrid aspen (Populus tremula 3 Populus tremuloides). A kinetic method based on dark release of isoprene emission at the expense of substrate pools accumulated in light was used to estimate the in vivo pool sizes of DMADP and upstream metabolites. Feeding with fosmidomycin, an inhibitor of DXP reductoisomerase, alone or in combination with bisphosphonates was used to inhibit carbon input into DXP/MEP pathway or both input and output. We observed a major increase in pathway intermediates, 3-to 4-fold, upstream of DMADP in bisphosphonateinhibited leaves, but the DMADP pool was enhanced much less, 1.3-to 1.5-fold. In combined fosmidomycin/bisphosphonate treatment, pathway intermediates accumulated, reflecting cytosolic flux of intermediates that can be important under strong metabolic pull in physiological conditions. The data suggested that metabolites accumulated upstream of DMADP consist of phosphorylated intermediates and IDP. Slow conversion of the huge pools of intermediates to DMADP was limited by reductive energy supply. These data indicate that the DXP/MEP pathway is extremely elastic, and the presence of a significant pool of phosphorylated intermediates provides an important valve for fine tuning the pathway flux.

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Isoprene Synthase Genes Form a Monophyletic Clade of Acyclic Terpene Synthases in the TPS-B Terpene Synthase Family

Cited by 91 publications

References 92 publications

Molecular cloning and biochemical characterization of isoprene synthases from the tropical trees Ficus virgata, Ficus septica, and Casuarina equisetifolia

Molecular cloning and biochemical characterization of isoprene synthases from the tropical trees Ficus virgata, Ficus septica, and Casuarina equisetifolia

Feedback Inhibition of Deoxy-d-xylulose-5-phosphate Synthase Regulates the Methylerythritol 4-Phosphate Pathway

Bisphosphonate Inhibitors Reveal a Large Elasticity of Plastidic Isoprenoid Synthesis Pathway in Isoprene-Emitting Hybrid Aspen

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