Harmark, K <br/><br/>
Substitution of aspartic acid-80, a residue involved in coordination of magnesium, weakens the GTP binding and strongly enhances the GTPase of the G domain of elongation factor Tu.  [electronic resource] 

 -  Biochemistry  Aug 1992 
 - 7367-72 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi00147a022  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Aspartic Acid<br/>Base Sequence<br/>Binding Sites<br/>Edetic Acid--pharmacology<br/>GTP Phosphohydrolase-Linked Elongation Factors--genetics<br/>Guanosine Diphosphate--metabolism<br/>Guanosine Triphosphate--metabolism<br/>Kinetics<br/>Magnesium--metabolism<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Oligodeoxyribonucleotides<br/>Peptide Elongation Factor Tu--genetics<br/>Protein Conformation