2016年9月
Molecular insights into the mechanism of thermal stability of actinomycete mannanase
FEBS LETTERS
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- 巻
- 590
- 号
- 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
- ID情報
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- DOI : 10.1002/1873-3468.12322
- ISSN : 0014-5793
- eISSN : 1873-3468
- Web of Science ID : WOS:000384807500006