folA Antibody

1. NADP+ not only binds to the native form but also a partially unfolded form of dihydrofolate reductase. PMID: 25367157
2. Quantum mechanics/molecular dynamics simulations reveal that the M20 loop conformational dynamics of dihydrofolate reductase (DHFR) is severely restricted at the transition state of the hydride transfer as a result of the M42W/G121V double mutation. PMID: 23297871
3. Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle PMID: 23614825
4. The data presented here provide a glimpse into the evolutionary trajectory of functional DHFR through its protein sequence space that lead to the diverged binding and catalytic properties of the E. coli and human enzymes. PMID: 23733948
5. Present a general kinetic framework that can be used to study conformation changes, apply this framework to E. coli DHFR and find the conformational change occurs predominantly prior to unbinding. PMID: 22641560
6. Protein interface remodeling in a chemically induced protein dimer. PMID: 22733548
7. Dihydrofolate reductase is bound to endogenous tetrahydrofolate PMID: 22024482
8. [review] A general mechanism is presented for folA catalysis that includes multiple intermediates and a complex, multidimensional standard free energy surface. PMID: 22029278
9. Only a single peptide from DHFR is found to be substantially more flexible than the Bacillus stearothermophilus-DHFR at 25 degrees C in a region located within the protein interior at the intersection of the cofactor and substrate-binding sites. PMID: 21859100
10. Taken together with previous studies in the millisecond time range, a hierarchical assembly of DHFR--in which each subdomain independently folds, subsequently docks, and then anneals into the native conformation after an initial global collapse--emerges. PMID: 21554889
11. Thermodynamics and solvent effects on substrate and cofactor binding in Escherichia coli chromosomal dihydrofolate reductase PMID: 21462996
12. mutant DHFR that abrogates millisecond-time-scale fluctuation in active site without perturbing structural and electrostatic preorganization; found link between conformational fluctuations on millisecond time scale and chemical step of enzymatic reaction PMID: 21474759
13. Fcused on residues 52, 67, 121, and 145 in the four distinct loops of DHFR. All the single-residue deletion mutants showed marked reduction in stability, except for Delta52 in an alphaC-betaC loop. PMID: 20045086
14. resulting triple mutants, DM-N18C, DM-R52C, DM-D87C and DM-D132C dihydrofolate reductase, were alkylated with glucose, N-acetylglucosamine, lactose and maltotriose iodoacetamides. PMID: 20412060
15. Data show that the M42W mutation alters the dynamics of DHFR and are consistent with theoretical analysis that suggests this mutation disrupts motion that promotes catalysis. PMID: 20073522
16. results suggest that dynamics in dihydrofolate reductase are exquisitely "tuned" for every intermediate in the catalytic cycle; structural fluctuations efficiently channel the enzyme through functionally relevant conformational space. PMID: 20080605
17. These results suggest that through electrostatic interactions Arg44 plays a functional role in retaining the cofactor binding affinity at the cost of the Escherichia coli dihydrofolate reductase stability. PMID: 20043879
18. Lys-32 residues have a role in the ionic interaction in R67 dihydrofolate reductase PMID: 15333636
19. the hydroxyl group of Tyr-69 of DFHR is important for interactions with NADPH, whereas both the hydroxyl group and hydrophobic ring atoms of the Tyr-69 residues are necessary for proper interactions with dihydrofolate PMID: 15333637
20. structural and functional alterations induced by peroxynitrite may play a direct role in compromising DHFR function in multiple pathological conditions PMID: 15639221
21. biophysical analysis of immobilized and native Escherichia coli dihydrofolate reductase PMID: 16258053
22. Results show that mutant dihydrofolate reductase has reduced catalytic activity. PMID: 16363797
23. characterization of higher energy conformational substates of dihydrofolate reductase using using nuclear magnetic resonance relaxation dispersion PMID: 16973882
24. DHFR structure from neutron diffraction studies provides insights into dynamics, active-site protonation states, and solvation pattern of the E. coli enzyme. PMID: 17130456
25. The folding trajectory of this alpha/beta-type protein (DHFR) is located between those of alpha-helical and beta-sheet proteins, suggesting that native structure determines the folding landscape. PMID: 17331539
26. Several mutations were found to grant resistance to trimethoprim, both by reducing the binding affinity of the enzyme for the drug, and by increasing the activity of the enzyme. PMID: 17451440

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KEGG: ecj:JW0047

STRING: 316385.ECDH10B_0049