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Structural insight into sugar-binding modes of microbial ß-amylase
https://tokushima-u.repo.nii.ac.jp/records/2012288
https://tokushima-u.repo.nii.ac.jp/records/20122888865b695-164a-4bf3-b1ee-a8f42b5f43d8
名前 / ファイル | ライセンス | アクション |
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Item type | 文献 / Documents(1) | |||||||||||||
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公開日 | 2024-11-20 | |||||||||||||
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アクセス権 | open access | |||||||||||||
アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||||||||||
資源タイプ | ||||||||||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||||||
資源タイプ | journal article | |||||||||||||
出版社版DOI | ||||||||||||||
識別子タイプ | DOI | |||||||||||||
関連識別子 | https://doi.org/10.1016/j.bbrc.2024.150695 | |||||||||||||
言語 | ja | |||||||||||||
関連名称 | 10.1016/j.bbrc.2024.150695 | |||||||||||||
出版タイプ | ||||||||||||||
出版タイプ | VoR | |||||||||||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||||||
タイトル | ||||||||||||||
タイトル | Structural insight into sugar-binding modes of microbial ß-amylase | |||||||||||||
言語 | en | |||||||||||||
著者 |
平田, 章
× 平田, 章
WEKO
1160
× Mikami, Bunzo
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抄録 | ||||||||||||||
内容記述タイプ | Abstract | |||||||||||||
内容記述 | ß-Amylase, which catalyses the release of ß-anomeric maltose from the non-reducing end of starch, is widely used in the food industry. Increasing its enzyme activity through protein engineering might improve the efficiency of food processing. To obtain detailed structural information to assist rationale design, here the crystal structure of Bacillus cereus β-amylase (BCB) complexed with maltose was determined by molecular replacement and refined using anisotropic temperature factors to 1.26 Å resolution with Rwork/Rfree factors of 12.4/15.7 %. The structure contains six maltose and one glucose molecules, of which two maltose and one glucose are bound at sites not previously observed in BCB structures. These three new sugar-binding sites are located on the surface and likely to be important in enhancing the degradation of raw-starch granules. In the active site of BCB, two maltose molecules are bound in tandem at subsites −2 ∼ −1 and +1 ∼ +2. Notably, the conformation of the glucose moiety bound at subsite −1 is a mixture of α-anomeric distorted 1,4B boat and 4C1 chair forms, while those at subsites −2, +1 ∼ +2 are all in the 4C1 chair forms. The O1 of the distorted α-glucose residue at subsite −1 occupies the position of the putative catalytic water, forming a hydrogen bond with OE1 of Glu367 (base catalyst), suggesting that this distorted sugar is not involved in catalysis. Together, these findings pave the way for further improving the functionality of microbial ß-amylase enzymes. | |||||||||||||
言語 | en | |||||||||||||
キーワード | ||||||||||||||
言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | β-amylase | |||||||||||||
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言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Bacillus cereus | |||||||||||||
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言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Raw-starch digestion | |||||||||||||
キーワード | ||||||||||||||
言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Novel sugar-binding sites | |||||||||||||
キーワード | ||||||||||||||
言語 | en | |||||||||||||
主題Scheme | Other | |||||||||||||
主題 | Distorted sugar formation | |||||||||||||
書誌情報 |
en : Biochemical and Biophysical Research Communications 巻 733, p. 150695, 発行日 2024-09-13 |
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収録物識別子タイプ | EISSN | |||||||||||||
収録物識別子 | 10902104 | |||||||||||||
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収録物識別子タイプ | PISSN | |||||||||||||
収録物識別子 | 0006291X | |||||||||||||
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収録物識別子タイプ | NCID | |||||||||||||
収録物識別子 | AA11542044 | |||||||||||||
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収録物識別子タイプ | NCID | |||||||||||||
収録物識別子 | AA00564395 | |||||||||||||
出版者 | ||||||||||||||
出版者 | Elsevier | |||||||||||||
言語 | en | |||||||||||||
権利情報 | ||||||||||||||
言語 | en | |||||||||||||
権利情報 | This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | |||||||||||||
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識別子 | 414434 | |||||||||||||
識別子タイプ | URI | |||||||||||||
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言語 | eng |