pubmed-article:2250652 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
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pubmed-article:2250652 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C0162801 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:2250652 | lifeskim:mentions | umls-concept:C0377068 | lld:lifeskim |
pubmed-article:2250652 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2250652 | pubmed:dateCreated | 1991-1-17 | lld:pubmed |
pubmed-article:2250652 | pubmed:abstractText | 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. | lld:pubmed |
pubmed-article:2250652 | pubmed:language | eng | lld:pubmed |
pubmed-article:2250652 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2250652 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2250652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2250652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2250652 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2250652 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2250652 | pubmed:month | Sep | lld:pubmed |
pubmed-article:2250652 | pubmed:issn | 0026-8925 | lld:pubmed |
pubmed-article:2250652 | pubmed:author | pubmed-author:StaudenbauerW... | lld:pubmed |
pubmed-article:2250652 | pubmed:author | pubmed-author:SchwarzW HWH | lld:pubmed |
pubmed-article:2250652 | pubmed:author | pubmed-author:JaurisSS | lld:pubmed |
pubmed-article:2250652 | pubmed:author | pubmed-author:RücknagelK... | lld:pubmed |
pubmed-article:2250652 | pubmed:author | pubmed-author:BronnenmeierK... | lld:pubmed |
pubmed-article:2250652 | pubmed:author | pubmed-author:KratzschPP | lld:pubmed |
pubmed-article:2250652 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2250652 | pubmed:volume | 223 | lld:pubmed |
pubmed-article:2250652 | pubmed:geneSymbol | celZ | lld:pubmed |
pubmed-article:2250652 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2250652 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2250652 | pubmed:pagination | 258-67 | lld:pubmed |
pubmed-article:2250652 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:2250652 | pubmed:meshHeading | pubmed-meshheading:2250652-... | lld:pubmed |
pubmed-article:2250652 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2250652 | pubmed:articleTitle | Sequence analysis of the Clostridium stercorarium celZ gene encoding a thermoactive cellulase (Avicelase I): identification of catalytic and cellulose-binding domains. | lld:pubmed |
pubmed-article:2250652 | pubmed:affiliation | Institute for Microbiology, Technical University Munich, Federal Republic of Germany. | lld:pubmed |
pubmed-article:2250652 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2250652 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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