| http://purl.uniprot.org/citations/19458657 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19458657 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19458657 | http://www.w3.org/2000/01/rdf-schema#comment | "In this study, the mining of an Antarctic soil sample by functional metagenomics allowed the isolation of a cold-adapted protein (RBcel1) that hydrolyzes only carboxymethyl cellulose. The new enzyme is related to family 5 of the glycosyl hydrolase (GH5) protein from Pseudomonas stutzeri (Pst_2494) and does not possess a carbohydrate-binding domain. The protein was produced and purified to homogeneity. RBcel1 displayed an endoglucanase activity, producing cellobiose and cellotriose, using carboxymethyl cellulose as a substrate. Moreover, the study of pH and the thermal dependence of the hydrolytic activity shows that RBcel1 was active from pH 6 to pH 9 and remained significantly active when temperature decreased (18% of activity at 10 degrees C). It is interesting that RBcel1 was able to synthetize non-reticulated cellulose using cellobiose as a substrate. Moreover, by a combination of bioinformatics and enzyme analysis, the physiological relevance of the RBcel1 protein and its mesophilic homologous Pst_2494 protein from P. stutzeri, A1501, was established as the key enzymes involved in the production of cellulose by bacteria. In addition, RBcel1 and Pst_2494 are the two primary enzymes belonging to the GH5 family involved in this process."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.org/dc/terms/identifier | "doi:10.1038/ismej.2009.48"xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.org/dc/terms/identifier | "doi:10.1038/ismej.2009.48"xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "D'Amico S."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "D'Amico S."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Feller G."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Feller G."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Galleni M."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Galleni M."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Power P."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Power P."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Berlemont R."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Berlemont R."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Delsaute M."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Delsaute M."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Pipers D."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/author | "Pipers D."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/name | "ISME J."xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/name | "ISME J"xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/pages | "1070-1081"xsd:string |
| http://purl.uniprot.org/citations/19458657 | http://purl.uniprot.org/core/pages | "1070-1081"xsd:string |