{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360846640214527872.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1007/s00253-011-3515-9"}},{"identifier":{"@type":"URI","@value":"http://link.springer.com/content/pdf/10.1007/s00253-011-3515-9.pdf"}},{"identifier":{"@type":"URI","@value":"http://link.springer.com/article/10.1007/s00253-011-3515-9/fulltext.html"}},{"identifier":{"@type":"URI","@value":"http://link.springer.com/content/pdf/10.1007/s00253-011-3515-9"}},{"identifier":{"@type":"PMID","@value":"21808968"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"Discovery of nigerose phosphorylase from Clostridium phytofermentans"}],"description":[{"notation":[{"@value":"A novel phosphorylase from Clostridium phytofermentans belonging to the glycoside hydrolase family (GH) 65 (Cphy1874) was characterized. The recombinant Cphy1874 protein produced in Escherichia coli showed phosphorolytic activity on nigerose in the presence of inorganic phosphate, resulting in the release of D-glucose and β-D-glucose 1-phosphate (β-G1P) with the inversion of the anomeric configuration. Kinetic parameters of the phosphorolytic activity on nigerose were k(cat) = 67 s(-1) and K(m) = 1.7 mM. This enzyme did not phosphorolyze substrates for the typical GH65 enzymes such as trehalose, maltose, and trehalose 6-phosphate except for a weak phosphorolytic activity on kojibiose. It showed the highest reverse phosphorolytic activity in the reverse reaction using D-glucose as the acceptor and β-G1P as the donor, and the product was mostly nigerose at the early stage of the reaction. The enzyme also showed reverse phosphorolytic activity, in a decreasing order, on D-xylose, 1,5-anhydro-D-glucitol, D-galactose, and methyl-α-D-glucoside. All major products were α-1,3-glucosyl disaccharides, although the reaction with D-xylose and methyl-α-D-glucoside produced significant amounts of α-1,2-glucosides as by-products. We propose 3-α-D-glucosyl-D-glucose:phosphate β-D-glucosyltransferase as the systematic name and nigerose phosphorylase as the short name for this Cphy1874 protein."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380284918415006337","@type":"Researcher","foaf:name":[{"@value":"Takanori Nihira"}]},{"@id":"https://cir.nii.ac.jp/crid/1380284918415006338","@type":"Researcher","foaf:name":[{"@value":"Hiroyuki Nakai"}]},{"@id":"https://cir.nii.ac.jp/crid/1380284918415006336","@type":"Researcher","foaf:name":[{"@value":"Kazuhiro Chiku"}]},{"@id":"https://cir.nii.ac.jp/crid/1380284918415006339","@type":"Researcher","foaf:name":[{"@value":"Motomitsu Kitaoka"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"01757598"},{"@type":"EISSN","@value":"14320614"}],"prism:publicationName":[{"@value":"Applied Microbiology and Biotechnology"}],"dc:publisher":[{"@value":"Springer Science and Business Media LLC"}],"prism:publicationDate":"2011-08-02","prism:volume":"93","prism:number":"4","prism:startingPage":"1513","prism:endingPage":"1522"},"reviewed":"false","dc:rights":["http://www.springer.com/tdm"],"url":[{"@id":"http://link.springer.com/content/pdf/10.1007/s00253-011-3515-9.pdf"},{"@id":"http://link.springer.com/article/10.1007/s00253-011-3515-9/fulltext.html"},{"@id":"http://link.springer.com/content/pdf/10.1007/s00253-011-3515-9"}],"createdAt":"2011-08-01","modifiedAt":"2024-04-09","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Clostridium","dc:title":"Clostridium"},{"@id":"https://cir.nii.ac.jp/all?q=Glycoside%20Hydrolases","dc:title":"Glycoside Hydrolases"},{"@id":"https://cir.nii.ac.jp/all?q=Phosphorylases","dc:title":"Phosphorylases"},{"@id":"https://cir.nii.ac.jp/all?q=Sequence%20Homology,%20Amino%20Acid","dc:title":"Sequence Homology, Amino Acid"},{"@id":"https://cir.nii.ac.jp/all?q=Gene%20Expression","dc:title":"Gene Expression"},{"@id":"https://cir.nii.ac.jp/all?q=Disaccharides","dc:title":"Disaccharides"},{"@id":"https://cir.nii.ac.jp/all?q=Recombinant%20Proteins","dc:title":"Recombinant Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Substrate%20Specificity","dc:title":"Substrate Specificity"},{"@id":"https://cir.nii.ac.jp/all?q=Molecular%20Weight","dc:title":"Molecular Weight"},{"@id":"https://cir.nii.ac.jp/all?q=Kinetics","dc:title":"Kinetics"},{"@id":"https://cir.nii.ac.jp/all?q=Escherichia%20coli","dc:title":"Escherichia coli"},{"@id":"https://cir.nii.ac.jp/all?q=Cloning,%20Molecular","dc:title":"Cloning, Molecular"},{"@id":"https://cir.nii.ac.jp/all?q=Phylogeny","dc:title":"Phylogeny"}],"project":[{"@id":"https://cir.nii.ac.jp/crid/1040000782188131584","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"23880010"},{"@type":"JGN","@value":"JP23880010"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-23880010/"}],"notation":[{"@language":"ja","@value":"新規糖質加リン酸分解酵素を活用した機能性オリゴ糖のライブラリー化"}]}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050008832572031104","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Structure of a bacterial α-1,2-glucosidase defines mechanisms of hydrolysis and substrate specificity in GH65 family hydrolases"}]},{"@id":"https://cir.nii.ac.jp/crid/1050025031477328128","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Characterization of a thermophilic 4-O-β-d-mannosyl-d-glucose phosphorylase fromRhodothermus marinus"},{"@value":"Characterization of a thermophilic 4-<i>O</i>-β-<scp>d</scp>-mannosyl-<scp>d</scp>-glucose phosphorylase from<i>Rhodothermus marinus</i>"},{"@value":"Characterization of a thermophilic 4-O-β-<sc>d</sc>-mannosyl-<sc>d</sc>-glucose phosphorylase from Rhodothermus marinus"}]},{"@id":"https://cir.nii.ac.jp/crid/1050025031480668544","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Metabolic Mechanism of Mannan in a Ruminal Bacterium, Ruminococcus albus, Involving Two Mannoside Phosphorylases and Cellobiose 2-Epimerase : Discovery of a New Carbohydrate Phosphorylase, β-1,4-Mannooligosaccharide Phosphorylase"},{"@value":"Metabolic Mechanism of Mannan in a Ruminal Bacterium, Ruminococcus albus, Involving Two Mannoside Phosphorylases and Cellobiose 2-Epimerase"},{"@value":"Metabolic mechanism of mannan in ruminal bacterium, Ruminococcuss albus, involving two mannoside phosphorylases and cellobiose 2-epimerase. 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機能性オリゴ糖の研究】　ホスホリラーゼ組み合わせ反応を用いた実用的オリゴ糖調製"},{"@language":"en","@value":"Special feature"},{"@value":"機能性オリゴ糖の研究 ホスホリラーゼ組み合わせ反応を用いた実用的オリゴ糖調製"},{"@language":"ja-Kana","@value":"キノウセイ オリゴトウ ノ ケンキュウ ホスホリラーゼ クミアワセ ハンノウ オ モチイタ ジツヨウテキ オリゴトウ チョウセイ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206292888960","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Purification and Characterization of a Novel Phosphorylase, Kojibiose Phosphorylase, from Thermoanaerobium brockii."},{"@language":"ja","@value":"Thermoanaerobiurn brockiiが産生する新規ホスホリラーゼ,コージビオースホスホリラーゼの精製とその諸性質"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206464037248","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Enzymatic synthesis of trehalose from maltose."}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206474065792","@type":"Article","resourceType":"学術雑誌論文(journal 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