Exploration and Structural Biology of Novel Enzymes from the GH31 Family
Author:
Affiliation:
1. Department of Bioscience, Graduate School of Science and Technology, Shizuoka University
2. Research Institute of Green Science and Technology, Shizuoka University
Publisher
The Japanese Society of Applied Glycoscience
Link
https://www.jstage.jst.go.jp/article/bag/14/2/14_92/_pdf
Reference50 articles.
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2. 2) C. Fanutti, M.J. Gidley, and J.S. Reid: A xyloglucan-oligosaccharide-specific α-D-xylosidase or exo-oligoxyloglucan-α-xylohydrolase from germinated nasturtium (Tropaeolum majus L.) seeds. Planta, 184, 137–147 (1991).
3. 3) H.J. Crombie, S. Chengappa, C. Jarman, C. Sidebottom, and J.S. Reid: Molecular characterisation of a xyloglucan oligosaccharide-acting α-D-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant ‘apoplastic’ α-D-glucosidases. Planta, 214, 406–413 (2002).
4. 4) S. Yu, K. Bojsen, B. Svensson, and J. Marcussen: α-1,4-Glucan lyases producing 1,5-anhydro-D-fructose from starch and glycogen have sequence similarity to α-glucosidases. Biochim. Biophys. Acta, 17, 1–15 (1999).
5. 5) A.L. Lovering, S.S. Lee, Y.W. Kim, S.G. Withers, and N.C. Strynadka: Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate. J. Biol. Chem., 280, 2105–2115 (2005).
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