Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding.
Open Access
- 1 February 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (4), 1738-1747
- https://doi.org/10.1016/s0021-9258(19)69870-4
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Interpretation of nuclear magnetic resonance spectra for Lactobacillus casei dihydrofolate reductase on the basis of the x-ray structure of the enzyme-methotrexate-NADPH complexBiochemistry, 1979
- Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymesBiochemistry, 1977
- Amino acid sequence of dihydrofolate reductase from an amethopterin‐resistant strain of Lactobacillus caseiFEBS Letters, 1977
- Dihydrofolate Reductase: X-ray Structure of the Binary Complex with MethotrexateScience, 1977
- The Amino‐Acid Sequence of the Dihydrofolate Reductase of a Trimethoprim‐Resistant Strain of Escherichia coliEuropean Journal of Biochemistry, 1977
- Purification and properties of Escherichia coli dihydrofolate reductaseBiochemistry, 1975
- Similarity in the Sequence of Escherichia coli Dihydrofolate Reductase with Other Pyridine Nucleotide-requiring EnzymesNature, 1974
- Estimation of dissociation constant of enzyme—ligand complex from fluorometric data by “difference” methodFEBS Letters, 1972
- Crystalline Dihydropteroylglutamic AcidNature, 1960
- Some comments on the Benesi‐Hildebrand equationRecueil des Travaux Chimiques des Pays-Bas, 1956