Gloss, L M <br/><br/>
Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191.  [electronic resource] 

 -  Proteins  Feb 1996 
 - 195-208 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0887-3585 
<br/><br/><label>Standard No.: </label>10.1002/(SICI)1097-0134(199602)24:2<195::AID-PROT6>3.0.CO;2-I  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alanine--chemistry<br/>Amino Acid Sequence<br/>Aspartate Aminotransferases--chemistry<br/>Conserved Sequence<br/>Cysteine--chemistry<br/>Escherichia coli--enzymology<br/>Models, Chemical<br/>Models, Molecular<br/>Mutagenesis, Site-Directed<br/>Mutation<br/>Protein Denaturation<br/>Structure-Activity Relationship<br/>Urea--pharmacology