Richter, Nina <br/><br/>
The three-dimensional structure of AKR11B4, a glycerol dehydrogenase from Gluconobacter oxydans, reveals a tryptophan residue as an accelerator of reaction turnover.  [electronic resource] 

 -  Journal of molecular biology  Dec 2010 
 - 353-62 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>1089-8638 
<br/><br/><label>Standard No.: </label>10.1016/j.jmb.2010.09.049  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Amino Acid Substitution<br/>Apraxia, Ideomotor<br/>Bacterial Proteins--chemistry<br/>Catalytic Domain--genetics<br/>Crystallography, X-Ray<br/>Gluconobacter oxydans--enzymology<br/>Hydrophobic and Hydrophilic Interactions<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>NADP--metabolism<br/>Protein Conformation<br/>Recombinant Proteins--chemistry<br/>Sequence Homology, Amino Acid<br/>Static Electricity<br/>Structural Homology, Protein<br/>Substrate Specificity<br/>Sugar Alcohol Dehydrogenases--chemistry<br/>Tryptophan--chemistry