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Origin, evolution, and divergence of plant class C GH9 endoglucanases

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dc.contributor.author Sharma, Rita
dc.date.accessioned 2024-08-01T08:58:59Z
dc.date.available 2024-08-01T08:58:59Z
dc.date.issued 2018-05
dc.identifier.uri https://bmcecolevol.biomedcentral.com/articles/10.1186/s12862-018-1185-2
dc.identifier.uri http://dspace.bits-pilani.ac.in:8080/jspui/xmlui/handle/123456789/15046
dc.description.abstract Glycoside 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.iso en en_US
dc.publisher Springer Nature en_US
dc.subject Biology en_US
dc.subject Glycoside hydrolases en_US
dc.subject CBM49 en_US
dc.subject Cellulases en_US
dc.title Origin, evolution, and divergence of plant class C GH9 endoglucanases en_US
dc.type Article en_US


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