2014年12月
Discovery of Two β-1,2-Mannoside Phosphorylases Showing Different Chain-Length Specificities from Thermoanaerobacter sp. X-514.
PLoS One
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- 巻
- 9
- 号
- 12
- 開始ページ
- e114882
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1371/journal.pone.0114882
We characterized Teth514_1788 and Teth514_1789, belonging to glycoside hydrolase family 130, from Thermoanaerobacter sp. X-514. These two enzymes catalyzed the synthesis of 1,2-β-oligomannan using β-1,2-mannobiose and d-mannose as the optimal acceptors, respectively, in the presence of the donor α-d-mannose 1-phosphate. Kinetic analysis of the phosphorolytic reaction toward 1,2-β-oligomannan revealed that these enzymes followed a typical sequential Bi Bi mechanism. The kinetic parameters of the phosphorolysis of 1,2-β-oligomannan indicate that Teth514_1788 and Teth514_1789 prefer 1,2-β-oligomannans containing a DP ≥3 and β-1,2-Man2, respectively. These results indicate that the two enzymes are novel inverting phosphorylases that exhibit distinct chain-length specificities toward 1,2-β-oligomannan. Here, we propose 1,2-β-oligomannan:phosphate α-d-mannosyltransferase as the systematic name and 1,2-β-oligomannan phosphorylase as the short name for Teth514_1788 and β-1,2-mannobiose:phosphate α-d-mannosyltransferase as the systematic name and β-1,2-mannobiose phosphorylase as the short name for Teth514_1789.
- リンク情報
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- DOI
- https://doi.org/10.1371/journal.pone.0114882
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/25500577
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000346375400058&DestApp=WOS_CPL
- 共同研究・競争的資金等の研究課題
- 複合糖鎖及びリポ多糖のホスホリラーゼ依存型新規代謝機構の解明
- 共同研究・競争的資金等の研究課題
- 生理機能の恒常性維持に有効な糖タンパク質の低コスト大量製造技術開発
- ID情報
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- DOI : 10.1371/journal.pone.0114882
- ISSN : 1932-6203
- PubMed ID : 25500577
- Web of Science ID : WOS:000346375400058