Structural Analysis of the Active Site Geometry of N5-Carboxyaminoimidazole Ribonucleotide Synthetase from Escherichia coli,
Author:
Affiliation:
1. Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, and Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, Michigan 48201
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi801734z
Reference26 articles.
1. Nucleic Acids, Purines, Pyrimidines (Nucleotide Synthesis)
2. Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway
3. N5-Carboxyaminoimidazole Ribonucleotide: Evidence for a New Intermediate and Two New Enzymic Activities in the de Novo Purine Biosynthetic Pathway of Escherichia coli
4. Evidence for the Direct Transfer of the Carboxylate of N5-Carboxyaminoimidazole Ribonucleotide (N5-CAIR) To Generate 4-Carboxy-5-aminoimidazole Ribonucleotide Catalyzed by Escherichia coli PurE, an N5-CAIR Mutase
5. Carboxylases in de Novo Purine Biosynthesis. Characterization of the Gallus gallus Bifunctional Enzyme
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