02293nas a2200253   4500008004100000022001400041245011800055210006900173260005700242300001400299490000700313520138200320653001301702653001501715653002401730653002301754100002601777700000901803700001801812700002701830700002401857700002701881856013101908       2013                        eng d  a0735-964000aFunctional characterization of a glucosyltransferase specific to flavonoid 7-O-glucosides from withania somnifera0 aFunctional characterization of a glucosyltransferase specific to  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcOCT  a1100-11080 v313 a<p>Flavonoids are a large class of phenylpropanoid-derived secondary metabolites, which are usually glycosylated by UDP-glycosyltransferases with one or more sugar groups. Here, we report the cloning and biochemical characterization of a flavonoid glycosyltransferase gene from Withania somnifera (WsGT), which is an important medicinal plant used in Ayurvedic formulations. Using PCR primers, designed for a highly conserved region of previously reported glycosyltransferases, we were able to isolate the corresponding fragment of the WsGT gene. Rapid amplification of cDNA ends (RACE) was then employed to isolate full-length cDNA, which had an open reading frame of 1,371 bp that encode for 456 amino acids. Phylogenetic analysis indicated that WsGT was similar to that of family 1 GT-B glycosyltransferase. Biochemical analysis revealed that WsGT interacts with UDP-glucose and was capable of regiospecifically glycosylating flavonoid-7-ols, such as apigenin, naringenin, luteolin, diadzein and genistein. Expression profiling studies showed that WsGT was highly expressed in young and mature leaves of W. somnifera. Furthermore, exposure to salicylic acid enhanced the expression of WsGT in the leaves and heat shock treatment resulted in decreased expression of WsGT after an initial increase. This may suggest the role of WsGT in response to abiotic/biotic stresses.</p>10aDiadzein10aFlavonoids10aGlycosyltransferase10aWithania somnifera1 aKumar, R., J. Santosh1 aRuby1 aSingh, Somesh1 aSonawane, Prashant, D.1 aVishwakarma, R., K.1 aKhan, Bashir, Mohammad  uhttp://library.ncl.res.in/content/functional-characterization-glucosyltransferase-specific-flavonoid-7-o-glucosides-withania-002269nas a2200241   4500008004100000022001400041245012300055210006900178260000900247300001200256490000800268520144100276653002701717653001501744653001101759653002901770653002101799100002501820700002201845700002001867700002001887856012001907       2021                        eng d  a0141-813000aFunctional insights into two Ocimum kilimandscharicum 4-coumarate-CoA ligases involved in phenylpropanoid biosynthesis0 aFunctional insights into two Ocimum kilimandscharicum 4coumarate  cJUN   a202-2100 v1813 a<p>Plant 4-coumarate-CoA ligase (4CL) catalyzes the ligation of CoA to cinnamic acid and its derivatives. Activated CoA esters are utilized for the biosynthesis of phenolic metabolites and lignin that play essential function in plants. Here, we characterize the diversity of Ocimum kilimandscharicum 4CLs (Ok4CLs). Phylogenetic analysis suggest that Ok4CLs could be grouped into three classes, class I -enzymes mostly involved in lignin biosynthesis, class II -non-structural phenylpropanoid biosynthesis and class III -yet to be characterized for specific role(s). We selected two Ok4CLs namely Ok4CL7 and Ok4CL15 for further characterization. Gene expression analysis sug-gested that Ok4CL7 is highly expressed in leaf trichomes, whereas Ok4CL15 is abundant in the roots. The recom-binant Ok4CL7 and Ok4CL15 had optimal enzyme activities at 40 degrees C in pH 8 and 7, respectively. Ok4CL7 showed substrate preference towards p-coumaric acid, ferulic acid and caffeic acid. While, Ok4CL15 preferredp-coumaric acid, ferulic acid and sinapic acid. Feruloyl adenylate showed higher number of contacts and lowers binding en-ergy with Ok4CL7 and 15 compared to cinnamoyl adenylate. Based on root-specific expression and preference for sinapic acid, Ok4CL15 might be involved in lignin biosynthesis. Further exploration is needed to unravel the role of diverse Ok4CLs in O. kilimandscharicum. (c) 2021 Elsevier B.V. All rights reserved.</p>10a4-Coumarate-CoA ligase10aFlavonoids10alignin10aOcimum kilimandscharicum10aPhenylpropanoids1 aLavhale, Santosh, G.1 aJoshi, Rakesh, S.1 aKumar, Yashwant1 aGiri, Ashok, P.  uhttp://library.ncl.res.in/content/functional-insights-two-ocimum-kilimandscharicum-4-coumarate-coa-ligases-involved