Bissaro, Bastien <br/><br/>
Mutation of a pH-modulating residue in a GH51 α-l-arabinofuranosidase leads to a severe reduction of the secondary hydrolysis of transfuranosylation products.  [electronic resource] 

 -  Biochimica et biophysica acta  Jan 2014 
 - 626-36 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-3002 
<br/><br/><label>Standard No.: </label>10.1016/j.bbagen.2013.10.013  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Arabinose--metabolism<br/>Bacillaceae--enzymology<br/>Catalysis<br/>Catalytic Domain<br/>Chromatography, Thin Layer<br/>Glycoside Hydrolases--chemistry<br/>Glycosylation<br/>Hydrogen-Ion Concentration<br/>Hydrolysis<br/>Kinetics<br/>Magnetic Resonance Spectroscopy<br/>Models, Molecular<br/>Mutagenesis, Site-Directed<br/>Mutation--genetics<br/>Substrate Specificity