Characterization of Glycosynthase Mutants Derived from Glycoside Hydrolase Family 10 Xylanases
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- SUGIMURA Masahiro
- Enzyme Laboratory, National Food Research Institute
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- NISHIMOTO Mamoru
- Enzyme Laboratory, National Food Research Institute
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- KITAOKA Motomitsu
- Enzyme Laboratory, National Food Research Institute
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抄録
Four xylanases belonging to glycoside hydrolase family 10—Thermotoga maritima XylB (TM), Clostridium stercorarium XynB (CS), Bacillus halodurans XynA (BH), and Cellulomonas fimi Cex (CF)—were converted to glycosynthases by substituting the nucleophilic glutamic acid residues with glycine, alanine, and serine. The glycine mutants exhibited the highest levels of glycosynthase activity with all four enzymes. All the glycine mutants formed polymeric β-1,4-linked xylopyranose as a precipitate during reaction with α-xylobiosyl fluoride. Two glycine mutants (TM and CF) recognized X2 as an effective acceptor molecule to prohibit the formation of the polymer, while the other two (CS and BH) did not. The difference in acceptor specificity is considered to reflect the difference in substrate affinity at their +2 subsites. The results agreed with the structural predictions of the subsite, where TM and CF exhibit high affinity at subsite 2, suggesting that the glycosynthase technique is useful for investigating the affinity of +subsites.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (5), 1210-1217, 2006
公益社団法人 日本農芸化学会
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詳細情報
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- CRID
- 1390282681453731328
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- NII論文ID
- 10018531432
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 7926368
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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
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- 使用不可