Johansson, Eva <br/><br/>
Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes.  [electronic resource] 

 -  The Journal of biological chemistry  Jan 2005 
 - 3051-9 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.M409534200  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alleles<br/>Amino Acid Sequence<br/>Arginine--chemistry<br/>Binding Sites<br/>Catalysis<br/>DNA Mutational Analysis<br/>Diffusion<br/>Dose-Response Relationship, Drug<br/>Escherichia coli--enzymology<br/>Genetic Vectors<br/>Glutamic Acid--chemistry<br/>Hydrolysis<br/>Magnesium--chemistry<br/>Methanococcus--enzymology<br/>Models, Chemical<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutation<br/>Nucleotide Deaminases--chemistry<br/>Phosphates--chemistry<br/>Protein Binding<br/>Protein Conformation<br/>Protein Structure, Secondary<br/>Salmonella typhimurium--enzymology<br/>Selenomethionine--chemistry<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity<br/>Thymidylate Synthase--chemistry