Hendle, J <br/><br/>
Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p).  [electronic resource] 

 -  Biochemistry  Apr 1995 
 - 4287-98 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/bi00013a018  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acetyltransferases--chemistry<br/>Amino Acid Sequence<br/>Asparagine--chemistry<br/>Azotobacter vinelandii--enzymology<br/>Binding Sites<br/>Catalysis<br/>Crystallization<br/>Crystallography, X-Ray<br/>Dihydrolipoyllysine-Residue Acetyltransferase<br/>Histidine--chemistry<br/>Hydrogen Bonding<br/>Hydrogen-Ion Concentration<br/>Kinetics<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Pyruvate Dehydrogenase Complex<br/>Serine--chemistry<br/>Structure-Activity Relationship