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Literature summary for 1.5.1.3 extracted from
- Differences in thermal structural changes and melting between mesophilic and thermophilic dihydrofolate reductase enzymes (2020), Phys. Chem. Chem. Phys., 22, 18361-18373 .
General Stability
| General Stability | Organism |
|---|---|
| are more mobile. Betweeen EcDHFR and TmDHFR there is a shift in melting temperature of 26 K | Escherichia coli |
| are more mobile. Betweeen EcDHFR and TmDHFR there is a shift in melting temperature of 26 K | Thermotoga maritima |
| comparison of the temperature dependence of stability and of flexibility between Thermotoga maritima and Escherichia coli enzymes. The TmDHFR dimer is overall not significantly more rigid than EcDHFR monomer. The TmDHFR protein core and most residues at the dimer interface exhibit smaller fluctuations than in EcDHFR, regions that are opposite to the interface | Escherichia coli |
| comparison of the temperature dependence of stability and of flexibility between Thermotoga maritima and Escherichia coli enzymes. The TmDHFR dimer is overall not significantly more rigid than EcDHFR monomer. The TmDHFR protein core and most residues at the dimer interface exhibit smaller fluctuations than in EcDHFR, regions that are opposite to the interface | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Thermotoga maritima | - |
- |
- |
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Release 2023.1 (January 2023)
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