Wille, Georg <br/><br/>
The role of Val-265 for flavin adenine dinucleotide (FAD) binding in pyruvate oxidase: FTIR, kinetic, and crystallographic studies on the enzyme variant V265A.  [electronic resource] 

 -  Biochemistry  Apr 2005 
 - 5086-94 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi047337o  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Base Sequence<br/>Catalytic Domain<br/>Crystallography, X-Ray<br/>DNA, Bacterial--genetics<br/>Flavin-Adenine Dinucleotide--metabolism<br/>Genetic Variation<br/>Kinetics<br/>Lactobacillus plantarum--enzymology<br/>Models, Molecular<br/>Mutagenesis, Site-Directed<br/>Oxidation-Reduction<br/>Protein Conformation<br/>Pyruvate Oxidase--chemistry<br/>Recombinant Proteins--chemistry<br/>Spectrophotometry<br/>Spectroscopy, Fourier Transform Infrared<br/>Valine--chemistry