Crystal structure of a neoagarobiose-producing GH16 family β-agarase from Persicobacter sp. CCB-QB2
Author:
Funder
Universiti Sains Malaysia
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s00253-019-10237-y.pdf
Reference32 articles.
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2. Allouch J, Helbert W, Henrissat B, Czjzek M (2004) Parallel substrate binding sites in a β-agarase suggest a novel mode of action on double-helical agarose. Structure 12:623–632. https://doi.org/10.1016/j.str.2004.02.020
3. An K, Shi X, Cui F, Cheng J, Liu N, Zhao X, Zhang XH (2018) Characterization and overexpression of a glycosyl hydrolase family 16 beta-agarase YM01-1 from marine bacterium Catenovulum agarivorans YM01T. Protein Expr Purif 143:1–8. https://doi.org/10.1016/j.pep.2017.10.002
4. Boratyn GM, Schaffer AA, Agarwala R, Altschul SF, Lipman DJ, Madden TL (2012) Domain enhanced lookup time accelerated BLAST. Biol Direct 7:12. https://doi.org/10.1186/1745-6150-7-12
5. Chi WJ, Park DY, Seo YB, Chang YK, Lee SY, Hong SK (2014) Cloning, expression, and biochemical characterization of a novel GH16 β-agarase AgaG1 from Alteromonas sp. GNUM-1. Appl Microbiol Biotechnol 98:4545–4555. https://doi.org/10.1007/s00253-014-5510-4
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