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タイトル: | Structure of β-1,4-mannanase from the common sea hare Aplysia kurodai at 1.05 Å resolution. |
著者: | Mizutani, Kimihiko https://orcid.org/0000-0002-1411-5429 (unconfirmed) Tsuchiya, Sae Toyoda, Mayuko Nanbu, Yuko Tominaga, Keiko Yuasa, Keizo Takahashi, Nobuyuki https://orcid.org/0000-0002-0196-8924 (unconfirmed) Tsuji, Akihiko Mikami, Bunzo |
著者名の別形: | 三上, 文三 |
キーワード: | mannanases hemicellulose secretory proteins |
発行日: | Oct-2012 |
出版者: | International Union of Crystallography |
誌名: | Acta crystallographica. Section F, Structural biology and crystallization communications |
巻: | 68 |
号: | Part 10 |
開始ページ: | 1164 |
終了ページ: | 1168 |
抄録: | 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. |
著作権等: | © 2012 International Union of Crystallography |
URI: | http://hdl.handle.net/2433/161049 |
DOI(出版社版): | 10.1107/S1744309112037074 |
PubMed ID: | 23027740 |
出現コレクション: | 学術雑誌掲載論文等 |
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