01800nas a2200229   4500008004100000022001400041245014700055210006900202260005700271300001200328490000700340520091600347653002501263653002501288653002101313653001801334653002201352100002601374700002201400700001601422856013201438       2006                        eng d  a0959-399300aRole of glucose in production and repression of polygalacturonase and pectate lyase from phytopathogenic fungus Fusarium moniliforme NCIM 12760 aRole of glucose in production and repression of polygalacturonas  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcSEP  a893-8990 v223 a<p>A mangrove fungal isolate Fusarium moniliforme NCIM 1276 was found to produce the maximum extracellular endopolygalacturonase and pectate lyase activities in liquid medium containing 1% citrus pectin and 0.2% glucose at pH 5 and pH 8, respectively. The enzyme secretion started after 10 h, when the spores were completely germinated, and maximum production occurred after 72 h in the extracellular medium. The production of polygalacturonase was enhanced by 0.2% glucose and completely repressed by 1% glucose. Pectate lyase secretion was also induced by a similar concentration of glucose in the extracellular medium and significantly decreased at 1% glucose. Quantification of extracellular and intracellular polygalacturonase and pectate lyase protein concentrations by ELISA and immunocytolocalization data suggested that glucose may control the expression of both enzymes at a transcriptional level.</p>10acatabolic repression10aFusarium moniliforme10ainducible enzyme10apectate lyase10apolygalacturonase1 aNiture, Suryakant, K.1 aKumar, Ameeta, R.1 aPant, Aditi  uhttps://library.ncl.res.in/content/role-glucose-production-and-repression-polygalacturonase-and-pectate-lyase-phytopathogenic-000938nas a2200229   4500008004100000022001400041245003900055210003900094260010600133300001400239490000700253520021800260653002800478653001900506653001800525653002300543653002200566653001300588100001700601700001900618856007100637       2007                        eng d  a0957-416600aFormal synthesis of herbarumin III0 aFormal synthesis of herbarumin III  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcJUL  a1688-16920 v183 a<p>An enantioselective synthesis of herbarumin III is described employing Jacobsen's hydrolytic kinetic resolution and Sharpless asymmetric dihydroxylation as the key steps. (c) 2007 Published by Elsevier Ltd.</p>10acarboxymethyl-cellulase10aF. moniliforme10apectate lyase10aplant pathogenesis10apolygalacturonase10aXylanase1 aGupta, Priti1 aKumar, Pradeep  uhttps://library.ncl.res.in/content/formal-synthesis-herbarumin-iii01504nas a2200193   4500008004100000022001400041245009000055210006900145260007900214300000900293490000700302520074600309653001801055653002301073653002201096653004201118100002601160856012401186       2008                        eng d  a0006-308800aComparative biochemical and structural characterizations of fungal polygalacturonases0 aComparative biochemical and structural characterizations of fung  aGENTHINER STRASSE 13, D-10785 BERLIN, GERMANYbWALTER DE GRUYTER GMBHcFEB  a1-190 v633 a<p>Endo- and exo-polygalacturonases produced by various fungi are involved in the degradation of pectic substances. They have found a wide range of applications in the food and textile industries. Several phyto-pathogenic fungi secrete polygalacturonases and they act as virulence factors during plant pathogenesis. The comparison of biochemical properties of different fungal polygalacturonases, their mechanism of actions, structural aspects and interactions with inhibitors/proteins could be used as a possible strategy for the fungal-crop disease management. This review focuses on fungal polygalacturonases, including their regulation, comparative biochemical and structural characterizations and their interactions with inhibitors.</p>10apectate lyase10aplant pathogenesis10apolygalacturonase10apolygalacturonase-inhibiting proteins1 aNiture, Suryakant, K.  uhttps://library.ncl.res.in/content/comparative-biochemical-and-structural-characterizations-fungal-polygalacturonases-002042nas a2200229   4500008004100000022001400041245016000055210006900215260009700284300001000381490000800391520111700399653002501516653001701541653001801558653002201576100002601598700002201624700002301646700001601669856012701685       2008                        eng d  a0944-501300aInactivation of polygalacturonase and pectate lyase produced by pH tolerant fungus Fusarium moniliforme NCIM 1276 in a liquid medium and in the host tissue0 aInactivation of polygalacturonase and pectate lyase produced by   aOFFICE JENA, P O BOX 100537, 07705 JENA, GERMANYbELSEVIER GMBH, URBAN & FISCHER VERLAGcJAN  a51-620 v1633 a<p>Fusarium moniliforme NCIM 1276 produced pH dependent an extracellular potygalacturonase (PG) and pectate lyase (PL) at pH 5 and pH 8, respectively. In the extracellular medium about 20.3% PG and 54% of PL protein concentrations were present in the active state at pH 5 and pH 8, respectively, whereas in intracelluarly, more than 86% of both protein contents remained in the active state at all pH tested. We found two possible reasons, end-product inhibition and effect of environmental. pH on conformation of the proteins after their release into the medium. Additionally, in infected tomato and cauliflower plants, the fungus secreted similar proteins which were located near to the epidermal and vascular regions of the hypocotyts. In infected tissues, between 26.9% and to 41.5% of PG and only 0.84% - 13.4% of PL protein concentrations were present in active state. Thus, the medium/cell sap pH and concentrations of substrate/end products seem to play an important role in fungal invasion during plant pathogenesis are discussed with current literature. (c) 2006 Elsevier GmbH. All rights reserved.</p>10aFusarium moniliforme10apathogenesis10apectate lyase10apolygatacturonase1 aNiture, Suryakant, K.1 aKumar, Ameeta, R.1 aParab, Pradeep, B.1 aPant, Aditi  uhttps://library.ncl.res.in/content/inactivation-polygalacturonase-and-pectate-lyase-produced-ph-tolerant-fungus-fusarium-0