Zuccotti, S <br/><br/>
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase.  [electronic resource] 

 -  Journal of molecular biology  Nov 2001 
 - 831-43 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.2001.5073  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Binding Sites<br/>Catalysis<br/>Crystallography, X-Ray<br/>Enzyme Inhibitors--chemistry<br/>Escherichia coli--enzymology<br/>Glucose--analogs & derivatives<br/>Glucosephosphates--metabolism<br/>Hydrogen Bonding<br/>Kinetics<br/>Models, Chemical<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Nucleotidyltransferases--antagonists & inhibitors<br/>Protein Structure, Quaternary<br/>Protein Structure, Tertiary<br/>Protein Subunits<br/>Recombinant Fusion Proteins--chemistry<br/>Rhamnose--metabolism<br/>Sequence Alignment<br/>Structure-Activity Relationship<br/>Thymine Nucleotides--metabolism