Crystal structure of a raw-starch-degrading bacterial α-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/srep44067.pdf
Reference42 articles.
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2. Liu, Y. et al. Identification and phylogenetic characterization of a new subfamily of alpha-amylase enzymes from marine microorganisms. Mar Biotechnol (NY) 14, 253–260, doi: 10.1007/s10126-011-9414-3 (2012).
3. Peng, H. et al. A starch-binding domain identified in alpha-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch. FEBS letters 588, 1161–1167, doi: 10.1016/j.febslet.2014.02.050 (2014).
4. Khemakhem, B. et al. The importance of an extra loop in the B-domain of an alpha-amylase from B. stearothermophilus US100. Biochemical and biophysical research communications 385, 78–83, doi: 10.1016/j.bbrc.2009.04.137 (2009).
5. Machius, M., Declerck, N., Huber, R. & Wiegand, G. Activation of Bacillus licheniformis alpha-amylase through a disorder–> order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6, 281–292 (1998).
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