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http://purl.uniprot.org/citations/26741138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26741138http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26741138http://www.w3.org/2000/01/rdf-schema#comment"With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70°C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0146454"xsd:string
http://purl.uniprot.org/citations/26741138http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0146454"xsd:string
http://purl.uniprot.org/citations/26741138http://purl.org/dc/terms/identifier"doi:10.1371/JOURNAL.PONE.0146454"xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Isupov M.N."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Isupov M.N."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Littlechild J.A."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Littlechild J.A."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Peng X."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Peng X."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Sayer C."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Sayer C."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Kolisis F.N."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Kolisis F.N."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Chatziioannou A."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Chatziioannou A."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Gudbergsdottir S.R."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Gudbergsdottir S.R."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Kissas D."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Kissas D."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Ladoukakis E."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Ladoukakis E."xsd:string
http://purl.uniprot.org/citations/26741138http://purl.uniprot.org/core/author"Skretas G."xsd:string