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Identification and characterization of a novel, versatile sialidase from a Sphingobacterium that can hydrolyze the glycosides of any sialic acid species at neutral pH
http://hdl.handle.net/2237/00032523
http://hdl.handle.net/2237/0003252300f2e7f4-48ea-49df-bb80-5b9ec01cdcc6
名前 / ファイル | ライセンス | アクション |
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BBRC-S-19-19643 (1.9 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2020-07-20 | |||||
タイトル | ||||||
タイトル | Identification and characterization of a novel, versatile sialidase from a Sphingobacterium that can hydrolyze the glycosides of any sialic acid species at neutral pH | |||||
言語 | en | |||||
著者 |
Iwaki, Yuya
× Iwaki, Yuya× Matsunaga, Emiko× Takegawa, Kaoru× Sato, Chihiro× Kitajima, Ken |
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アクセス権 | ||||||
アクセス権 | open access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
権利 | ||||||
言語 | en | |||||
権利情報 | © 2020. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Sialidase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Kdn-sialidase | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Neutral pH | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Sphingobacterium | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Sialic acid | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | Deaminoneuraminic acid | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Bacterial sialidases are widely used to remove sialic acid (Sia) residues from glycans. Most of them cleave the glycosides of N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc) under acidic pHs; however, currently available bacterial sialidases had no activity to the glycosides of deaminoneuraminic acid (Kdn). In this study, we found a novel sialidase from Sphingobacterium sp. strain HMA12 that could cleave any of the glycosides of Neu5Ac, Neu5Gc, and Kdn. It also had a broad linkage specificity, i.e., α2,3-, α2,6-, α2,8-, and α2,9-linkages, and the optimal pH at neutral ranges, pH 6.5–7.0. These properties are particularly important when sialidases are applied for in vivo digestion of the cell surface sialosides under physiological conditions. Interestingly, 2,3-didehydro-2-deoxy-N-acetylneuraminic acid (Neu5Ac2en), which is a transition state analog-based inhibitor, competitively inhibited the enzyme-catalyzed reaction for Kdn as well as for Neu5Ac, suggesting that the active site is common to the Neu5Ac and Kdn residues. Taken together, this sialidase is versatile and useful for the in vivo research on sialo-glycoconjugates. | |||||
言語 | en | |||||
内容記述 | ||||||
内容記述タイプ | Other | |||||
内容記述 | ファイル公開:2021-03-05 | |||||
言語 | ja | |||||
出版者 | ||||||
出版者 | Elsevier | |||||
言語 | en | |||||
言語 | ||||||
言語 | eng | |||||
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 | |||||
出版タイプ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1016/j.bbrc.2019.12.079 | |||||
ISSN(print) | ||||||
収録物識別子タイプ | PISSN | |||||
収録物識別子 | 0006-291X | |||||
書誌情報 |
en : Biochemical and Biophysical Research Communications 巻 523, 号 2, p. 487-492, 発行日 2020-03-05 |
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著者版フラグ | ||||||
値 | author |