論文

査読有り
2016年9月

Molecular insights into the mechanism of thermal stability of actinomycete mannanase

FEBS LETTERS
  • Yuya Kumagai
  • ,
  • Misugi Uraji
  • ,
  • Kun Wan
  • ,
  • Masayuki Okuyama
  • ,
  • Atsuo Kimura
  • ,
  • Tadashi Hatanaka

590
17
開始ページ
2862
終了ページ
2869
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/1873-3468.12322
出版者・発行元
WILEY-BLACKWELL

Streptomyces thermolilacinus mannanase (StMan), which requires Ca2+ for its enhanced thermal stability and hydrolysis activity, possesses two Ca2+-binding sites in loop6 and loop7. We evaluated the function of the Ca2+-binding site in loop7 and the hydrogen bond between residues Ser247 in loop6 and Asp279 in loop7. The Ca2+-binding in loop7 was involved only in thermal stability. Mutations of Ser247 or Asp279 retained the Ca2+-binding ability; however, mutants showed less thermal stability than StMan. Phylogenetic analysis indicated that most glycoside hydrolase family 5 subfamily 8 mannanases could be stabilized by Ca2+; however, the mechanism of StMan thermal stability was found to be quite specific in some actinomycete mannanases.

リンク情報
DOI
https://doi.org/10.1002/1873-3468.12322
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000384807500006&DestApp=WOS_CPL
ID情報
  • DOI : 10.1002/1873-3468.12322
  • ISSN : 0014-5793
  • eISSN : 1873-3468
  • Web of Science ID : WOS:000384807500006

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