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dc.contributor.author | Mizutani, Kimihiko | en |
dc.contributor.author | Tsuchiya, Sae | en |
dc.contributor.author | Toyoda, Mayuko | en |
dc.contributor.author | Nanbu, Yuko | en |
dc.contributor.author | Tominaga, Keiko | en |
dc.contributor.author | Yuasa, Keizo | en |
dc.contributor.author | Takahashi, Nobuyuki | en |
dc.contributor.author | Tsuji, Akihiko | en |
dc.contributor.author | Mikami, Bunzo | en |
dc.contributor.alternative | 三上, 文三 | ja |
dc.date.accessioned | 2012-11-08T06:18:07Z | - |
dc.date.available | 2012-11-08T06:18:07Z | - |
dc.date.issued | 2012-10 | - |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | http://hdl.handle.net/2433/161049 | - |
dc.description.abstract | β-1,4-Mannanase (EC 3.2.1.78) catalyzes the hydrolysis of β-1,4-glycosidic bonds within mannan, a major constituent group of the hemicelluloses. Bivalves and gastropods possess β-1,4-mannanase and may degrade mannan in seaweed and/or phytoplankton to obtain carbon and energy using the secreted enzymes in their digestive systems. In the present study, the crystal structure of AkMan, a gastropod β-1,4-mannanase prepared from the common sea hare Aplysia kurodai, was determined at 1.05 Å resolution. This is the first report of the three-dimensional structure of a gastropod β-1,4-mannanase. The structure was compared with bivalve β-1,4-mannanase and the roles of residues in the catalytic cleft were investigated. No obvious binding residue was found in subsite +1 and the substrate-binding site was exposed to the molecular surface, which may account for the enzymatic properties of mannanases that can digest complex substrates such as glucomannan and branched mannan. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | International Union of Crystallography | en |
dc.rights | © 2012 International Union of Crystallography | en |
dc.subject | mannanases | en |
dc.subject | hemicellulose | en |
dc.subject | secretory proteins | en |
dc.title | Structure of β-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 Å resolution. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA12097708 | - |
dc.identifier.jtitle | Acta crystallographica. Section F, Structural biology and crystallization communications | en |
dc.identifier.volume | 68 | - |
dc.identifier.issue | Part 10 | - |
dc.identifier.spage | 1164 | - |
dc.identifier.epage | 1168 | - |
dc.relation.doi | 10.1107/S1744309112037074 | - |
dc.textversion | publisher | - |
dc.identifier.pmid | 23027740 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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