Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Organ / tissue: pellicle
NCBI PubMed ID: 8110656Journal NLM ID: 7909578Publisher: Butterworth-Heinemann
Institutions: Department of Microbiology, University of British Columbia, Vancouver, Canada
Endo-β-1,4-glucanase A (CenA), a cellulase from the bacterium Cellulomonas fimi, is composed of two domains: a catalytic domain and a cellulose-binding domain. Adsorption of CenA and its isolated cellulose-binding domain (CBD.PTCenA) to Valonia cellulose microcrystals was examined by transmission electron microscopy using an antibody sandwich technique (CenA/CBD.PTCenA-α CenA IgG-protein A-gold conjugate). Adsorption of both CenA and CBD.PTCenA occurred along the lengths of the microcrystals, with an apparent preference for certain crystal faces or edges. CenA or CBD.PTCenA, but not the isolated catalytic domain, were shown to prevent the flocculation of microcrystalline bacterial cellulose. The cellulose-binding domain may assist crystalline cellulose hydrolysis in vitro by promoting substrate dispersion.
Structure type: homopolymer
Trivial name: cellulose, β-(1,4)-glucan, cellulose, β-(1,4)-glucan
Compound class: EPS, O-polysaccharide, cell wall polysaccharide, glucan, polysaccharide
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
Comments, role: Parent molecule: cellulose
Related record ID(s): 112991
NCBI Taxonomy refs (TaxIDs): 28448Reference(s) to other database(s): GTC:G75830OM, GlycomeDB:
27885, CCSD:
50051, CBank-STR:4229
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There is only one chemically distinct structure:
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(later renamed to: Komagataeibacter xylinus)