Southall, Stacey M <br/><br/>
Soluble aldose sugar dehydrogenase from Escherichia coli: a highly exposed active site conferring broad substrate specificity.  [electronic resource] 

 -  The Journal of biological chemistry  Oct 2006 
 - 30650-9 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M601783200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acinetobacter calcoaceticus--enzymology<br/>Aspartate-Semialdehyde Dehydrogenase<br/>Binding Sites<br/>Calcium--metabolism<br/>Carbohydrate Dehydrogenases--chemistry<br/>Escherichia coli--enzymology<br/>Escherichia coli Proteins<br/>Gluconates--chemistry<br/>Glucose--chemistry<br/>Glucose 1-Dehydrogenase--chemistry<br/>Hydrogen-Ion Concentration<br/>Hydrolysis<br/>Models, Molecular<br/>PQQ Cofactor--chemistry<br/>Protein Structure, Secondary<br/>Substrate Specificity