Ramón-Maiques, S <br/><br/>
The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases.  [electronic resource] 

 -  Journal of molecular biology  Jun 2000 
 - 463-76 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.2000.3779  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Diphosphate--metabolism<br/>Amino Acid Sequence<br/>Binding Sites<br/>Carbamyl Phosphate--metabolism<br/>Catalysis<br/>Crystallography, X-Ray<br/>Dimerization<br/>Enterococcus faecalis--enzymology<br/>Enzyme Stability<br/>Kinetics<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Phosphotransferases (Carboxyl Group Acceptor)--chemistry<br/>Protein Binding<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Pyrococcus furiosus--enzymology<br/>Solvents<br/>Static Electricity<br/>Structure-Activity Relationship<br/>Temperature