Ito, Ryousuke <br/><br/>
β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade.  [electronic resource] 

 -  Organic & biomolecular chemistry  Jun 2014 
 - 3836-46 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1477-0539 
<br/><br/><label>Standard No.: </label>10.1039/c4ob00064a  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Chromatography, Gas<br/>Cyclization<br/>Electrons<br/>Euphorbia--enzymology<br/>Intramolecular Transferases--metabolism<br/>Mutagenesis, Site-Directed<br/>Mutant Proteins--chemistry<br/>Oleanolic Acid--analogs & derivatives<br/>Phenylalanine--chemistry<br/>Structure-Activity Relationship<br/>Substrate Specificity