01812nas a2200169   4500008004100000022001400041245011800055210006900173260011000242300001400352490000700366520106400373100001901437700002101456700003701477856012801514       2013                        eng d  a1463-926200aBiocatalysis: fungi mediated novel and selective 12 beta- or 17 beta-hydroxylation on the basic limonoid skeleton0 aBiocatalysis fungi mediated novel and selective 12 beta or 17 be  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcMAR  a1311-13170 v153 a<p>Basic limonoids carrying a 4,4,8-trimethyl-17-furanylsteroid skeleton are a class of triterpenoids and well-known for their insecticidal as well as a vast array of pharmacological activities. Rare and synthetically challenging 12 beta- and 17 beta-hydroxylation was achieved on the basic limonoid skeleton to produce a novel series of hydroxylated limonoids using fungi-mediated biocatalysis. The fungal system belonging to the genera of Mucor efficiently converted azadiradione, epoxyazadiradione, gedunin and their derivatives into corresponding 12 beta- and/or 17 beta-hydroxy derivatives. The position and stereochemistry of hydroxylation was determined by rigorous spectroscopic and crystallographic studies. This fungi-mediated stereo- and regio-selective hydroxylation process was highly efficient and mild enough to sustain chemically sensitive functional groups around the basic limonoid skeleton. Modifications of specific functional groups and variation in biocatalyst were shown to bring selectivity among 12 beta- or 17 beta-hydroxylation.</p>1 aHaldar, Saikat1 aKolet, Swati, P.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/biocatalysis-fungi-mediated-novel-and-selective-12-beta-or-17-beta-hydroxylation-basic-001870nas a2200229   4500008004100000022001400041245010100055210006900156260007900225300001400304490000700318520099500325653002501320653002201345653001401367100002101381700002701402700001901429700002401448700003701472856013101509       2013                        eng d  a0039-128X00aBiocatalyst mediated production of 6 beta,11 alpha-dihydroxy derivatives of 4-ene-3-one steroids0 aBiocatalyst mediated production of 6 beta11 alphadihydroxy deriv  a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcNOV  a1152-11580 v783 a<p>Biotransformation of steroids with 4-ene-3-one functionality such as progesterone (I), testosterone (II), 17 alpha-methyltestosterone (III), 4-androstene-3,17-dione (IV) and 19-nortestosterone (V) were studied by using a fungal system belonging to the genera of Mucor (M881). The fungal system efficiently and quantitatively converted these steroids in regio- and stereo-selective manner into corresponding 6 beta,11 alpha-dihydroxy compounds. Time course experiments suggested that the transformation was initiated by hydroxylation at 6 beta- or 11 alpha-(10 beta-hydroxy in case of V) to form monohydroxy derivatives which upon prolonged incubation were converted into corresponding 613,11oc-dihydroxy derivatives. The fermentation studies carried out using 5 L table-top fermentor with substrates (I and II) clearly indicates that 6 beta,11 alpha-dihydroxy derivatives of steroids with 4-ene-3-one functionality can be produced in large scale by using M881. (C) 2013 Elsevier Ltd.</p>10a4-Ene-3-one steroids10aBiotransformation10aMucor sp.1 aKolet, Swati, P.1 aNiloferjahan, Siddiqui1 aHaldar, Saikat1 aGonnade, Rajesh, G.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/biocatalyst-mediated-production-6-beta11-alpha-dihydroxy-derivatives-4-ene-3-one-steroids-001193nas a2200181   4500008004100000022001400041245010300055210006900158260011000227300001400337490000600351520042200357100001900779700002400798700002100822700003700843856013100880       2013                        eng d  a1759-966000aExpedient preparative isolation, quantification and characterization of limonoids from neem fruits0 aExpedient preparative isolation quantification and characterizat  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcAUG  a5386-53910 v53 a<p>Major basic limonoids from Neem fruits such as azadirone, epoxyazadiradione and azadiradione were isolated in preparative scale using an automated and rapid medium pressure liquid chromatography (MPLC)-based protocol. They were individually quantified using HPLC. An LC-ESI-MS/MS-based rapid identification technique was developed for the high-throughput screening of these limonoids in phytochemical extracts.</p>1 aHaldar, Saikat1 aPhapale, Prasad, B.1 aKolet, Swati, P.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/expedient-preparative-isolation-quantification-and-characterization-limonoids-neem-fruits-001600nas a2200217   4500008004100000022001400041245009400055210006900149260007100218300001600289490000700305520078500312100001901097700001901116700002101135700002301156700001801179700002101197700003701218856012701255       2013                        eng d  a0022-326300aOne-pot fluorescent labeling protocol for complex hydroxylated bioactive natural products0 aOnepot fluorescent labeling protocol for complex hydroxylated bi  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcOCT  a10192-102020 v783 a<p>Tagging of small bioactive molecules with a fluorophore is a highly sensitive method to trace their cellular activities through real-time visual information. Here we disclose a 7-nitrobenzo-2-oxa-1,3-diazole (NBD)-based, high-yielding, one-pot labeling protocol for hydroxylated molecules using Yamaguchi coupling as the key reaction. This methodology was successfully applied on several sensitive and complex hydroxylated bioactive compounds including 7-deacetylazadiradione, simvastatin, camptothecin, andrographolide, cinchonine, beta-dihydroartemisinin, and azadirachtin A. Further, utility of this protocol was illustrated on the cytotoxic activity of azadiradione derivatives against several cancer cell lines through cell imaging of two qualified fluorescent probes.</p>1 aHaldar, Saikat1 aKumar, Santosh1 aKolet, Swati, P.1 aPatil, Harshal, S.1 aKumar, Dhiraj1 aKundu, Gopal, C.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/one-pot-fluorescent-labeling-protocol-complex-hydroxylated-bioactive-natural-products-001282nas a2200205   4500008004100000022001400041245008100055210006900136260011000205300001600315490000600331520047900337100001900816700002100835700002700856700002100883700002400904700003700928856011100965       2014                        eng d  a2046-206900aBiocatalyst mediated functionalization of salannin, an insecticidal limonoid0 aBiocatalyst mediated functionalization of salannin an insecticid  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcJUN  a27661-276640 v43 a<p>Transformation of salannin, an insecticidal C-seco limonoid was investigated using a fungal system, Cunninghamella echinulata. Salannin was efficiently converted into two metabolites, where the C-17 furan moiety was transformed into gamma-hydroxybutenolide (salanninolide) and N-(2-hydroxyethyl)-alpha,beta-unsaturated-gamma-lactam (salanninactam) analogues. Present studies have indicated salanninolide to be a metabolite in the C-seco limonoid biosynthetic pathway.</p>1 aHaldar, Saikat1 aKolet, Swati, P.1 aDandekar, Devdutta, S.1 aKale, Balaji, S.1 aGonnade, Rajesh, G.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/biocatalyst-mediated-functionalization-salannin-insecticidal-limonoid-001309nas a2200181   4500008004100000022001400041245010500055210006900160260011000229300001400339490000700353520052600360100002500886700003100911700002100942700003700963856012701000       2014                        eng d  a1477-052000aBiocatalyst mediated regio- and stereo-selective hydroxylation and epoxidation of (Z)-alpha-santalol0 aBiocatalyst mediated regio and stereoselective hydroxylation and  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcJAN  a1048-10510 v123 a<p>Biocatalyst mediated regio- and stereo-selective hydroxylation and epoxidation on (Z)-alpha-santalol were achieved for the first time, using a fungal strain Mucor piriformis. Four novel metabolites were characterized as 10,11-cis-beta-epoxy-alpha-santalol, 5 alpha-hydroxy-(Z)-alpha-santalol, 10,11-dihydroxy-alpha-santalol and 5 alpha-hydroxy-10,11-cis-beta-epoxy-alpha-santalol. Using Amano PS lipase from Burkholderia cepacia, alpha- and beta-isomers of 10,11-cis-epoxy-alpha-santalol were resolved efficiently.</p>1 aDaramwar, Pankaj, P.1 aSrivastava, Prabhakar, Lal1 aKolet, Swati, P.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/biocatalyst-mediated-regio-and-stereo-selective-hydroxylation-and-epoxidation-z-alpha-001490nas a2200253   4500008004100000022001400041245008400055210006900139260010600208300001400314490000700328520053700335653002800872653002100900653002200921653002300943653002000966100002100986700002301007700002901030700002801059700003701087856011201124       2014                        eng d  a0040-403900aFungi mediated production and practical purification of (R)-(-)-3-quinuclidinol0 aFungi mediated production and practical purification of R3quinuc  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcOCT  a5911-59140 v553 a<p>A fungal system belonging to Mucoraceae family (Mucor piriformis) was explored for the asymmetric reduction of a prochiral ketone, 3-quinuclidinone (I) in an efficient manner to produce an important pharmaceutical precursor (R)-(-)-3-quinuclidinol (II) with similar to 96% enantiomeric excess. The efficiency of the process was improved by developing a cation exchange resin (Amberlite IR-120) which assisted the purification of water soluble metabolite II from fermentation media. (C) 2014 Elsevier Ltd. All rights reserved.</p>10a(R)-(-)-3-Quinuclidinol10aAmberlite IR-12010aBiotransformation10aIon exchange resin10aMucor pinformis1 aKolet, Swati, P.1 aJadhav, Dipesh, D.1 aPriyadarshini, Balaraman1 aSwarge, Bhagyashree, N.1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/fungi-mediated-production-and-practical-purification-r-3-quinuclidinol-001674nas a2200241   4500008004100000022001400041245013300055210006900188260007900257300000900336490000700345520074600352653002501098653002201123653001901145653001701164653001701181100002101198700001901219700002701238700003701265856013001302       2014                        eng d  a0039-128X00aMucor hiemalis mediated 14 alpha-hydroxylation on steroids: In vivo and in vitro investigations of 14 alpha-hydroxylase activity0 aMucor hiemalis mediated 14 alphahydroxylation on steroids In viv  a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcJUL  a6-120 v853 a<p>Transformation of testosterone and progesterone into synthetically challenging 14 alpha-hydroxy derivatives was achieved by using fungal strain Mucor hiemalis. Prolonged incubation led to the formation of corresponding 6 beta/7 alpha,14 alpha-dihydroxy metabolites. The position and stereochemistry of newly introduced hydroxyl group was determined by detailed spectroscopic analyses. The time course experiment indicated that fungal strain initiated transformation by hydroxylation at 14 alpha-position followed by at 6 beta- or 7 alpha-positions. Studies using cell-free extracts suggest that the 14 alpha-hydroxylase activity is NADPH dependent and belongs to the cytochrome P450 family. (C) 2014 Elsevier Inc. All rights reserved.</p>10a14 alpha-Hydroxylase10aBiotransformation10aMucor hiemalis10aProgesterone10aTestosterone1 aKolet, Swati, P.1 aHaldar, Saikat1 aNiloferjahan, Siddiqui1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/mucor-hiemalis-mediated-14-alpha-hydroxylation-steroids-vivo-and-vitro-investigations-14-002317nas a2200217   4500008004100000022001400041245014200055210006900197260009000266300002500356490000600381520140900387100002701796700003101823700001601854700002101870700002401891700001901915700003701934856012801971       2015                        eng d  a2045-232200aCharacterization of 10-hydroxygeraniol dehydrogenase from catharanthus roseus reveals cascaded enzymatic activity in iridoid biosynthesis0 aCharacterization of 10hydroxygeraniol dehydrogenase from cathara  aMACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLANDbNATURE PUBLISHING GROUPcFEB  aArticle Number: 82580 v53 a<p>Catharanthus roseus [L.] is a major source of the monoterpene indole alkaloids (MIAs), which are of significant interest due to their therapeutic value. These molecules are formed through an intermediate, cis-trans-nepetalactol, a cyclized product of 10-oxogeranial. One of the key enzymes involved in the biosynthesis of MIAs is an NAD(P)(+) dependent oxidoreductase system, 10-hydroxygeraniol dehydrogenase (Cr10HGO), which catalyses the formation of 10-oxogeranial from 10-hydroxygeraniol via 10-oxogeraniol or 10-hydroxygeranial. This work describes the cloning and functional characterization of Cr10HGO from C. roseus and its role in the iridoid biosynthesis. Substrate specificity studies indicated that, Cr10HGO has good activity on substrates such as 10-hydroxygeraniol, 10-oxogeraniol or 10-hydroxygeranial over monohydroxy linear terpene derivatives. Further it was observed that incubation of 10-hydroxygeraniol with Cr10HGO and iridoid synthase (CrIDS) in the presence of NADP(+) yielded a major metabolite, which was characterized as (1R, 4aS, 7S, 7aR)-nepetalactol by comparing its retention time, mass fragmentation pattern, and co-injection studies with that of the synthesized compound. These results indicate that there is concerted activity of Cr10HGO with iridoid synthase in the formation of (1R, 4aS, 7S, 7aR)-nepetalactol, an important intermediate in iridoid biosynthesis.</p>1 aKrithika, Ramakrishnan1 aSrivastava, Prabhakar, Lal1 aRani, Bajaj1 aKolet, Swati, P.1 aChopade, Manojkumar1 aSoniya, Mantri1 aThulasiram, Hirekodathakallu, V.  uhttps://library.ncl.res.in/content/characterization-10-hydroxygeraniol-dehydrogenase-catharanthus-roseus-reveals-cascaded-102869nas a2200253   4500008004100000022001400041245012500055210006900180260009000249300001200339490000700351520190100358653001802259653002402277653002102301653003402322653001902356653001102375100001802386700002102404700003702425700002102462856013202483       2015                        eng d  a0885-576500aRole of methyl jasmonate in the expression of mycorrhizal induced resistance against Fusarium oxysporum in tomato plants0 aRole of methyl jasmonate in the expression of mycorrhizal induce  a24-28 OVAL RD, LONDON NW1 7DX, ENGLANDbACADEMIC PRESS LTD- ELSEVIER SCIENCE LTDcOCT  a139-1450 v923 a<p>Arbuscular mycorrhiza (AM) colonization led to a decrease in the severity of fusarium wilt disease caused by Fusarium oxysporum f. sp. lycopersici in tomato plants. The involvement of two plant defense hormones, namely methyl jasmonate (MeJA) and salicylic acid (SA), in the expression of mycorrhiza induced resistance (MIR) against this vascular pathogen was studied in the AM colonized and non-colonized (controls) plants. Activity of lipoxygenase (LOX), which plays a role in jasmonic acid (JA) biosynthesis, as well as levels of methyl jasmonate (MeJA) increased in AM colonized plants as compared to controls, but did not show any further changes in response to F. oxysporum inoculation. On the other hand, activity of phenylalanine ammonia lyase (PAL), which is an enzyme from salicylic acid (SA) biosynthetic pathway, as well as SA levels, increased in both controls and AM colonized plants in response to application of F. oxysporum spores. Hence the JA and not the SA signalling pathway appeared to play a role in the expression of MIR against this vascular pathogen. The resistance observed in AM colonized plants was completely compromised when plants were treated with the JA biosynthesis inhibitor salicylhydroxamic acid (SHAM). This confirmed that the AM-induced increase in JA levels was involved in the expression of resistance toward F. oxysporum. The SA response gene pathogenesis-related 1 (PR1) showed an increased expression in response to F. oxysporum infection in SHAM treated AM colonized plants as compared to plants that were not treated with this JA inhibitor. This suggested the possibility that JA inhibited SA responses, at least in the roots. AM colonization therefore appeared to prime plants for improved tolerance against the vascular pathogen F. oxysporum, which was mediated through the JA signalling pathway. (C) 2015 Elsevier Ltd. All rights reserved.</p>10aFusarium wilt10aGlomus fasciculatum10aMethyl jasmonate10aMycorrhiza induced resistance10aSalicylic acid10aTomato1 aNair, Aswathy1 aKolet, Swati, P.1 aThulasiram, Hirekodathakallu, V.1 aBhargava, Sujata  uhttps://library.ncl.res.in/content/role-methyl-jasmonate-expression-mycorrhizal-induced-resistance-against-fusarium-oxysporum-002807nas a2200265   4500008004100000022001400041245013100055210006900186260006700255300001200322490000700334520184400341653002502185653002002210653002302230653002102253653002702274653001902301653002502320100001302345700002102358700002302379700001702402856012202419       2015                        eng d  a1435-860300aSystemic jasmonic acid modulation in mycorrhizal tomato plants and its role in induced resistance against alternaria alternata0 aSystemic jasmonic acid modulation in mycorrhizal tomato plants a  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcMAY  a625-6310 v173 a<p>Tomato plants colonised with the arbuscular mycorrhizal (AM) fungus Glomus fasciculatum show systemic induced resistance to the foliar pathogen Alternaria alternata, as observed in interactions of other AM-colonised plants with a range of pathogens. The role of jasmonic (JA) and salicylic (SA) acid in expression of this mycorrhiza-induced resistance (MIR) against A.alternata was studied by measuring: (i) activity of enzymes reported to be involved in their biosynthesis, namely lipoxygenase (LOX) and phenylammonia lyase (PAL); and (ii) levels of methyl jasmonate (MeJA) and SA. Transcript abundance of some defence genes associated with JA and SA response pathways were also studied. Both LOX and PAL activity increased twofold in response to pathogen application to control plants. AM-colonised plants had three-fold higher LOX activity compared to control plants, but unlike controls, this did not increase further in response to pathogen application. Higher LOX activity in AM-colonised plants correlated with four-fold higher MeJA in leaves of AM-colonised plants compared to controls. Treatment of plants with the JA biosynthesis inhibitor salicylhydroxamic acid (SHAM) led to 50% lower MeJA in both control and AM-colonised plants and correlated with increased susceptibility to A.alternata, suggesting a causal role for JA in expression of MIR against the pathogen. Genes involved in JA biosynthesis (OPR3) and response (COI1) showed six- and 42-fold higher expression, respectively, in leaves of AM-colonised plants compared to controls. AM-colonised plants also showed increased expression of the SA response gene PR1 and that of the wound-inducible polypeptide prosystemin. Our results suggest that the systemic increase in JA in response to AM colonisation plays a key role in expression of MIR against A. alternata.</p>10aAlternaria alternata10aAM colonisation10ainduced resistance10aMethyl jasmonate10asalicylhydroxamic acid10aSalicylic acid10aSolanum lycopersicum1 aNair, A.1 aKolet, Swati, P.1 aThulasiram, H., V.1 aBhargava, S.  uhttps://library.ncl.res.in/content/systemic-jasmonic-acid-modulation-mycorrhizal-tomato-plants-and-its-role-induced-0