Structure and function of endoglucanase V View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-09

AUTHORS

Gideon J. Davies, G. Guy Dodson, Roderick E. Hubbard, Shirley P. Tolley, Zbigniew Dauter, Keith S. Wilson, Carsten Hjort, Jan Møller Mikkelsen, Grethe Rasmussen, Martin Schülein

ABSTRACT

CELLULOSE is the major polysaccharide component of plant cell walls and is the most abundant organic compound on the planet. A number of bacterial1 and fungal2 organisms can use cellulose as a food source, possessing cellulases (cellobiohydrolases and endoglucanases) that can catalyse the hydrolysis of the β-(1,4) glycosidic bonds. They can be classified into seven distinct families3. The three-dimensional structures of members of two of these families are known4,5. Here we report the structure of a third cellulase, endoglucanase V, whose sequence is not represented in any of the above families. The enzyme is structurally distinct from the previously determined cellulases but is similar to a recently characterized plant defence protein6. The active site region resembles that of lysozyme, despite the lack of structural similarity between these two enzymes. More... »

PAGES

362-364

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/365362a0

DOI

http://dx.doi.org/10.1038/365362a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009393837

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8377830


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