Differences in the Substrate Specificities and Active-Site Structures of Two α-L-Fucosidases (Glycoside Hydrolase Family 29) from Bacteroides thetaiotaomicron
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- SAKURAMA Haruko
- Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
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- TSUTSUMI Erika
- Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
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- ASHIDA Hisashi
- Graduate School of Biostudies, Kyoto University Graduate School of Biostudies, Kyoto University
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- KATAYAMA Takane
- Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
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- YAMAMOTO Kenji
- Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
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- KUMAGAI Hidehiko
- Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University
書誌事項
- タイトル別名
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- Differences in the Substrate Specificities and Active-Site Structures of Two α-<small>L</small>-Fucosidases (Glycoside Hydrolase Family 29) from <i>Bacteroides thetaiotaomicron</i>
- Differences in the Substrate Specificities and Active-Site Structures of Two α-<scp>L</scp>-Fucosidases (Glycoside Hydrolase Family 29) from<i>Bacteroides thetaiotaomicron</i>
- Differences in the substrate specificities and active-site structures of two a-L-fucosidases (glycoside hydrolase Family 29) from Bacteroids thetaiotaomicron
- Differences in the substrate specificities and active-site structures of two α-L-fucosidases (glycoside hydrolase family 29) from Bacteroids thetaiotaomicron
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抄録
Recent studies suggest that α-L-fucosidases of glycoside hydrolase family 29 can be divided into two subfamilies based on substrate specificity and phylogenetic clustering. To explore the validity of this classification, we enzymatically characterized two structure-solved α-L-fucosidases representing the respective subfamilies. Differences in substrate specificities are discussed in relation to differences in active-site structures between the two enzymes.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 76 (5), 1022-1024, 2012
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681455017728
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- NII論文ID
- 10030753211
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- NII書誌ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC38jltlOmtg%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 023682044
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- PubMed
- 22738979
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可