Kopečný, David <br/><br/>
Carboxylate and aromatic active-site residues are determinants of high-affinity binding of ω-aminoaldehydes to plant aminoaldehyde dehydrogenases.  [electronic resource] 

 -  The FEBS journal  Sep 2011 
 - 3130-9 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1742-4658 
<br/><br/><label>Standard No.: </label>10.1111/j.1742-4658.2011.08239.x  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Aldehyde Oxidoreductases--chemistry<br/>Aldehydes--metabolism<br/>Amino Acids, Aromatic--metabolism<br/>Amino Acids, Dicarboxylic--metabolism<br/>Betaine--analogs & derivatives<br/>Biocatalysis<br/>Catalytic Domain<br/>Circular Dichroism<br/>Isoenzymes--metabolism<br/>Kinetics<br/>Mutagenesis, Site-Directed<br/>Mutant Proteins--chemistry<br/>Pisum sativum--enzymology<br/>Plant Proteins--chemistry<br/>Propylamines--metabolism<br/>Protein Structure, Secondary<br/>Recombinant Proteins--chemistry<br/>Substrate Specificity