Fernandes, A C <br/><br/>
Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes.  [electronic resource] 

 -  The Biochemical journal  Aug 1999 
 - 105-10 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0264-6021 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acetylation<br/>Amidohydrolases--chemistry<br/>Bacterial Proteins--chemistry<br/>Binding Sites<br/>Catalytic Domain<br/>Cellulose--analogs & derivatives<br/>Cloning, Molecular<br/>Clostridium--enzymology<br/>Enzyme Stability<br/>Genes, Bacterial--genetics<br/>Hydrogen-Ion Concentration<br/>Hydrolysis<br/>Kinetics<br/>Ligands<br/>Multienzyme Complexes--chemistry<br/>Sequence Deletion<br/>Sequence Homology, Amino Acid<br/>Solubility<br/>Substrate Specificity<br/>Temperature<br/>Xylan Endo-1,3-beta-Xylosidase<br/>Xylans--metabolism<br/>Xylosidases--chemistry