@article { ISI:000241361400002, title = {Role of glucose in production and repression of polygalacturonase and pectate lyase from phytopathogenic fungus Fusarium moniliforme NCIM 1276}, journal = {World Journal of Microbiology \& Biotechnology}, volume = {22}, number = {9}, year = {2006}, month = {SEP}, pages = {893-899}, publisher = {SPRINGER}, type = {Article}, address = {233 SPRING ST, NEW YORK, NY 10013 USA}, abstract = {

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.

}, keywords = {catabolic repression, Fusarium moniliforme, inducible enzyme, pectate lyase, polygalacturonase}, issn = {0959-3993}, doi = {10.1007/s11274-006-9119-3}, author = {Niture, Suryakant K. and Kumar, Ameeta R. and Pant, Aditi} } @article {sanjayan, title = {Formal synthesis of herbarumin III}, journal = {Tetrahedron-Asymmetry}, volume = {18}, number = {14}, year = {2007}, month = {JUL}, pages = {1688-1692}, publisher = {PERGAMON-ELSEVIER SCIENCE LTD}, type = {Article}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND}, abstract = {

An enantioselective synthesis of herbarumin III is described employing Jacobsen{\textquoteright}s hydrolytic kinetic resolution and Sharpless asymmetric dihydroxylation as the key steps. (c) 2007 Published by Elsevier Ltd.

}, keywords = {carboxymethyl-cellulase, F. moniliforme, pectate lyase, plant pathogenesis, polygalacturonase, Xylanase}, issn = {0957-4166}, doi = {10.1016/j.tetasy.2007.07.022}, author = {Gupta, Priti and Kumar, Pradeep} } @article { ISI:000252539500001, title = {Comparative biochemical and structural characterizations of fungal polygalacturonases}, journal = {Biologia}, volume = {63}, number = {1}, year = {2008}, month = {FEB}, pages = {1-19}, publisher = {WALTER DE GRUYTER GMBH}, type = {Article}, address = {GENTHINER STRASSE 13, D-10785 BERLIN, GERMANY}, abstract = {

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.

}, keywords = {pectate lyase, plant pathogenesis, polygalacturonase, polygalacturonase-inhibiting proteins}, issn = {0006-3088}, doi = {10.2478/s11756-008-0018-y}, author = {Niture, Suryakant K.} }