Liu, Sijiu <br/><br/>
Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution.  [electronic resource] 

 -  Biochemistry  Mar 2005 
 - 2949-62 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi0479712  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Carbon-Carbon Lyases--chemistry<br/>Catalysis<br/>Cloning, Molecular<br/>Conserved Sequence<br/>Crystallography, X-Ray<br/>Escherichia coli--enzymology<br/>Escherichia coli Proteins--chemistry<br/>Evolution, Molecular<br/>Kinetics<br/>Magnesium--metabolism<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Protein Binding<br/>Protein Conformation<br/>Protein Structure, Secondary<br/>Recombinant Proteins--chemistry<br/>Salmonella typhimurium--enzymology<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity