Site-directed mutagenesis to probe catalysis by a Thermobifida fusca -1,3-glucanase (Lam81A)
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/22/6/375/4367174/gzp015.pdf
Reference21 articles.
1. Eng1p, an Endo-1,3-β-Glucanase Localized at the Daughter Side of the Septum, Is Involved in Cell Separation in Saccharomyces cerevisiae
2. The Conformation of the Tri- and Tetrasaccharide Produced in the Hydrolysis of Barley Glucan with the Enzyme Endo-1,3-1,4-β-glucan 4-Glucanohydrolase fromBacillus Licheniformis
3. Separation of [1-3H]cellooligosaccharides by thin-layer chromatography: Assay for cellulolytic enzymes
4. Catalytic properties of the bifunctional soybean β-glucan-binding protein, a member of family 81 glycoside hydrolases
5. Structural Basis for the Substrate Specificity of a Bacillus 1,3-1,4-β-Glucanase
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3. Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2009-2010;Mass Spectrometry Reviews;2014-05-26
4. The cellulolytic system ofThermobifida fusca;Critical Reviews in Microbiology;2013-03-28
5. Characterization and identification of essential residues of the glycoside hydrolase family 64 laminaripentaose-producing- -1, 3-glucanase;Protein Engineering Design and Selection;2011-06-25
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