02972nas a2200313   4500008004100000022001400041245010400055210006900159260010300228300001200331490000700343520187800350653001302228653002102241653001002262653003502272653002102307653002202328100001802350700001802368700002502386700001902411700001802430700002502448700001902473700002002492700001702512856012902529       2013                        eng d  a0981-942800aCharacterization of three novel isoprenyl diphosphate synthases from the terpenoid rich mango fruit0 aCharacterization of three novel isoprenyl diphosphate synthases   a23 RUE LINOIS, 75724 PARIS, FRANCEbELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIERcOCT  a121-1310 v713 a<p>Mango (cv. Alphonso) is popular due to its highly attractive, terpenoid-rich flavor. Although Alphonso is clonally propagated, its fruit-flavor composition varies when plants are grown in different geo-climatic zones. Isoprenyl diphosphate synthases catalyze important branch-point reactions in terpenoid biosynthesis, providing precursors for common terpenoids such as volatile terpenes, sterols and carotenoids. Two geranyl diphosphate synthases and a farnesyl diphosphate synthase were isolated from Alphonso fruits, cloned for recombinant expression and found to produce the respective products. Although, one of the geranyl diphosphate synthases showed high sequence similarity to the geranylgeranyl diphosphate synthases, it did not exhibit geranylgeranyl diphosphate synthesizing activity. When modeled, this geranyl diphosphate synthase and farnesyl diphosphate synthase structures were found to be homologous with the reference structures, having all the catalytic side chains appropriately oriented. The optimum temperature for both the geranyl diphosphate synthases was 40 degrees C and that for farnesyl diphosphate synthase was 25 degrees C. This finding correlated well with the dominance of monoterpenes in comparison to sesquiterpenes in the fruits of Alphonso mango in which the mesocarp temperature is higher during ripening than development. The absence of activity of these enzymes with the divalent metal ion other than Mg2+ indicated their adaptation to the Mg2+ rich mesocarp. The typical expression pattern of these genes through the ripening stages of fruits from different cultivation localities depicting the highest transcript levels of these genes in the stage preceding the maximum terpene accumulation indicated the involvement of these genes in the biosynthesis of volatile terpenes. (C) 2013 Elsevier Masson SAS. All rights reserved.</p>10aAlphonso10aFlavor variation10aFruit10aIsoprenyl diphosphate synthase10aMangifera indica10aTerpene volatiles1 aKulkarni, Ram1 aPandit, Sagar1 aChidley, Hemangi, G.1 aNagel, Raimund1 aSchmidt, Axel1 aGershenzon, Jonathan1 aPujari, Keshav1 aGiri, Ashok, P.1 aGupta, Vidya  uhttps://library.ncl.res.in/content/characterization-three-novel-isoprenyl-diphosphate-synthases-terpenoid-rich-mango-fruit-002496nas a2200289   4500008004100000022001400041245011300055210006900168260009300237300000800330490000600338520148200344653001901826653002501845653001101870653002101881653001301902100001801915700002501933700002201958700001801980700001901998700002002017700002502037700001702062856012702079       2013                        eng d  a2193-180100aOxidoreductase from `Alphonso' mango catalyzing biosynthesis of furaneol and reduction of reactive carbonyls0 aOxidoreductase from Alphonso mango catalyzing biosynthesis of fu  aGEWERBESTRASSE 11, CHAM, CH-6330, SWITZERLANDbSPRINGER INTERNATIONAL PUBLISHING AGcOCT  a4940 v23 a<p>Two furanones, furaneol (4-hydroxy-2,5-dimethyl-3(2H)-furanone) and mesifuran (2,5-dimethyl-4-methoxy-3(2H)-furanone), are important constituents of flavor of the Alphonso cultivar of mango (Mangifera indica). To get insights into the biosynthesis of these furanones, we isolated an enone oxidoreductase gene from the Alphonso mango. It has high sequence similarity to an alkenal/one oxidoreductase from cucumber (79% identity) and enone oxidoreductases from tomato (73% identity) and strawberry (72% identity). The complete open reading frame was expressed in E. coli and the (his) 6-tagged recombinant protein was purified by affinity chromatography. The purified protein assayed with NADH as a reducing agent converted D-fructose-1,6-diphosphate into furaneol, the immediate precursor of mesifuran. The enzyme was also able to convert two highly reactive carbonyls, 3-buten-2-one and 1-penten-3-one, produced by lipid peroxidation in plants, into their saturated derivatives. Expression profiling in various ripening stages of Alphonso fruits depicted an expression maxima at 10 days after harvest stage, shortly before the appearance of the maximum amount of furanones (completely ripe stage, 15 days after harvest). Although no furanones were detected at the 0 day after harvest stage, significant expression of this gene was detected in the fruits at this stage. Overall, the results suggest that this oxidoreductase plays important roles in Alphonso mango fruits.</p>10aDetoxification10aEnone oxidoreductase10aFlavor10aMangifera indica10aRipening1 aKulkarni, Ram1 aChidley, Hemangi, G.1 aDeshpande, Ashish1 aSchmidt, Axel1 aPujari, Keshav1 aGiri, Ashok, P.1 aGershenzon, Jonathan1 aGupta, Vidya  uhttps://library.ncl.res.in/content/oxidoreductase-alphonso-mango-catalyzing-biosynthesis-furaneol-and-reduction-reactive-0