Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. The Biochemistry of Folic Acid and Related Pteridines;Blakley,1969
2. Similarity in the Sequence of Escherichia coli Dihydrofolate Reductase with Other Pyridine Nucleotide-requiring Enzymes
3. Amino-Acid Sequence of Dihydrofolate Reductase from a Methotrexate-resistant Mutant of Streptococcus faecium and Identification of Methionine Residues at the Inhibitor Binding Site
4. Amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain ofLactobacillus casei
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1. Thermodynamics and Solvent Effects on Substrate and Cofactor Binding in Escherichia coli Chromosomal Dihydrofolate Reductase;Biochemistry;2011-04-15
2. Structural comparison of chromosomal and exogenous dihydrofolate reductase fromStaphylococcus aureusin complex with the potent inhibitor trimethoprim;Proteins: Structure, Function, and Bioinformatics;2009-08-15
3. Mutational ‘hot-spots’ in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: Sequence and structural comparison;Drug Resistance Updates;2009-02
4. Increasing Methotrexate Resistance by Combination of Active-site Mutations in Human Dihydrofolate Reductase;Journal of Molecular Biology;2007-10
5. Substrate and inhibitor specificity of Mycobacterium avium dihydrofolate reductase;FEBS Journal;2007-06-03
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