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http://purl.uniprot.org/citations/11577723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11577723http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11577723http://www.w3.org/2000/01/rdf-schema#comment"The intracellular beta-xylosidase was induced when Streptomyces thermoviolaceus OPC-520 was grown at 50 degrees C in a minimal medium containing xylan or xylooligosaccharides. The 82-kDa protein with beta-xylosidase activity was partially purified and its N-terminal amino acid sequence was analyzed. The gene encoding the enzyme was cloned, sequenced, and expressed in Escherichia coli. The bxlA gene consists of a 2,100-bp open reading frame encoding 770 amino acids. The deduced amino acid sequence of the bxlA gene product had significant similarity with beta-xylosidases classified into family 3 of glycosyl hydrolases. The bxlA gene was expressed in E. coli, and the recombinant protein was purified to homogeneity. The enzyme was a monomer with a molecular mass of 82 kDa. The purified enzyme showed hydrolytic activity towards only p-nitrophenyl-beta-D-xylopyranoside among the synthetic glycosides tested. Thin-layer chromatography analysis showed that the enzyme is an exo-type enzyme that hydrolyze xylooligosaccharides, but had no activity toward xylan. High activity against pNPX occurred in the pH range 6.0-7.0 and temperature range 40-50 degrees C."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.org/dc/terms/identifier"doi:10.1271/bbb.65.1824"xsd:string
http://purl.uniprot.org/citations/11577723http://purl.org/dc/terms/identifier"doi:10.1271/bbb.65.1824"xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Miyamoto K."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Miyamoto K."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Tsuji A."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Tsuji A."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Kosaka M."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Kosaka M."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Inamori Y."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Inamori Y."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Tsujibo H."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Tsujibo H."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Takada C."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/author"Takada C."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/name"Biosci. Biotechnol. Biochem."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/name"Biosci Biotechnol Biochem"xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/pages"1824-1831"xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/pages"1824-1831"xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/title"Cloning, sequencing, and expression of the gene encoding an intracellular beta-D-xylosidase from Streptomyces thermoviolaceus OPC-520."xsd:string
http://purl.uniprot.org/citations/11577723http://purl.uniprot.org/core/title"Cloning, sequencing, and expression of the gene encoding an intracellular beta-D-xylosidase from Streptomyces thermoviolaceus OPC-520."xsd:string