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  1. H180 生物機能開発利用研究センター
  2. H180a 雑誌掲載論文
  3. 学術雑誌

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/2237/00032523
00f2e7f4-48ea-49df-bb80-5b9ec01cdcc6
名前 / ファイル ライセンス アクション
BBRC-S-19-19643.pdf BBRC-S-19-19643 (1.9 MB)
Item type 学術雑誌論文 / Journal Article(1)
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

WEKO 100673

en Iwaki, Yuya

Search repository
Matsunaga, Emiko

× Matsunaga, Emiko

WEKO 100674

en Matsunaga, Emiko

Search repository
Takegawa, Kaoru

× Takegawa, Kaoru

WEKO 100675

en Takegawa, Kaoru

Search repository
Sato, Chihiro

× Sato, Chihiro

WEKO 100676

en Sato, Chihiro

Search repository
Kitajima, Ken

× Kitajima, Ken

WEKO 100677

en Kitajima, Ken

Search repository
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 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
内容記述タイプ Abstract
内容記述
内容記述 ファイル公開:2021-03-05
言語 ja
内容記述タイプ Other
出版者
言語 en
出版者 Elsevier
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
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
著者版フラグ
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