Negative cooperativity between folinic acid and coenzyme in their binding to L. casei dihydrofolate reductase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00528a021
Reference35 articles.
1. Effects of halides on reduced nicotinamide adenine dinucleotide binding properties and catalytic activity of beef heart lactate dehydrogenase
2. The Mechanism of Interaction of Red Cell Organic Phosphates with Hemoglobin
3. Reciprocal binding of oxygen and diphosphoglycerate by human hemoglobin.
4. Cooperativity in ligand binding to dihydrofolate reductase
5. Binding of coenzyme analogs to Lactobacillus casei dihydrofolate reductase: binary and ternary complexes
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3. NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions;Biochemistry;2011-04-14
4. Structure and dynamics in solution of the complex of lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate;Protein Science;2008-12-31
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