http://purl.uniprot.org/citations/2250652 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2250652 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2250652 | http://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/2250652 | http://purl.org/dc/terms/identifier | "doi:10.1007/bf00265062"xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.org/dc/terms/identifier | "doi:10.1007/bf00265062"xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.org/dc/terms/identifier | "doi:10.1007/BF00265062"xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Bronnenmeier K."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Bronnenmeier K."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Staudenbauer W.L."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Staudenbauer W.L."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Schwarz W.H."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Schwarz W.H."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Jauris S."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Jauris S."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Ruecknagel K.P."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Ruecknagel K.P."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Kratzsch P."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/author | "Kratzsch P."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/name | "Mol. Gen. Genet."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/name | "Mol. Gen. Genet."xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/pages | "258-267"xsd:string |
http://purl.uniprot.org/citations/2250652 | http://purl.uniprot.org/core/pages | "258-267"xsd:string |
http://purl.uniprot.org/citations/2250652 | http://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 |