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http://purl.uniprot.org/citations/2250652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2250652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2250652http://www.w3.org/2000/01/rdf-schema#comment"The nucleotide sequence of the celZ gene coding for a thermostable endo-beta-1,4-glucanase (Avicelase I) of Clostridium stercorarium was determined. The structural gene consists of an open reading frame of 2958 bp which encodes a preprotein of 986 amino acids with an Mr of 109,000. The signal peptide cleavage site was identified by comparison with the N-terminal amino acid sequence of Avicelase I purified from C. stercorarium culture supernatants. The recombinant protein expressed in Escherichia coli is proteolytically cleaved into catalytic and cellulose-binding fragments of about 50 kDa each. Sequence comparison revealed that the N-terminal half of Avicelase I is closely related to avocado (Persea americana) cellulase. Homology is also observed with Clostridium thermocellum endoglucanase D and Pseudomonas fluorescens cellulase. The cellulose-binding region was located in the C-terminal half of Avicelase I. It consists of a reiterated domain of 88 amino acids flanked by a repeated sequence about 140 amino acids in length. The C-terminal flanking sequence is highly homologous to the non-catalytic domain of Bacillus subtilis endoglucanase and Caldocellum saccharolyticum endoglucanase B. It is proposed that the enhanced cellulolytic activity of Avicelase I is due to the presence of multiple cellulose-binding sites."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.org/dc/terms/identifier"doi:10.1007/bf00265062"xsd:string
http://purl.uniprot.org/citations/2250652http://purl.org/dc/terms/identifier"doi:10.1007/bf00265062"xsd:string
http://purl.uniprot.org/citations/2250652http://purl.org/dc/terms/identifier"doi:10.1007/BF00265062"xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Bronnenmeier K."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Bronnenmeier K."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Staudenbauer W.L."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Staudenbauer W.L."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Schwarz W.H."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Schwarz W.H."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Jauris S."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Jauris S."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Ruecknagel K.P."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Ruecknagel K.P."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Kratzsch P."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/author"Kratzsch P."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/name"Mol. Gen. Genet."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/name"Mol. Gen. Genet."xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/pages"258-267"xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/pages"258-267"xsd:string
http://purl.uniprot.org/citations/2250652http://purl.uniprot.org/core/title"Sequence analysis of the Clostridium stercorarium celZ gene encoding a thermoactive cellulase (Avicelase I): identification of catalytic and cellulose-binding domains."xsd:string