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dc.contributor.authorSharma, Rita-
dc.date.accessioned2024-08-01T08:58:59Z-
dc.date.available2024-08-01T08:58:59Z-
dc.date.issued2018-05-
dc.identifier.urihttps://bmcecolevol.biomedcentral.com/articles/10.1186/s12862-018-1185-2-
dc.identifier.urihttp://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/15046-
dc.description.abstractGlycoside hydrolases of the GH9 family encode cellulases that predominantly function as endoglucanases and have wide applications in the food, paper, pharmaceutical, and biofuel industries. The partitioning of plant GH9 endoglucanases, into classes A, B, and C, is based on the differential presence of transmembrane, signal peptide, and the carbohydrate binding module (CBM49). There is considerable debate on the distribution and the functions of these enzymes which may vary in different organisms. In light of these findings we examined the origin, emergence, and subsequent divergence of plant GH9 endoglucanases, with an emphasis on elucidating the role of CBM49 in the digestion of crystalline cellulose by class C members.en_US
dc.language.isoenen_US
dc.publisherSpringer Natureen_US
dc.subjectBiologyen_US
dc.subjectGlycoside hydrolasesen_US
dc.subjectCBM49en_US
dc.subjectCellulasesen_US
dc.titleOrigin, evolution, and divergence of plant class C GH9 endoglucanasesen_US
dc.typeArticleen_US
Appears in Collections:Department of Biological Sciences

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