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Literature summary for 1.5.1.3 extracted from
- Effect of dimerization on the stability and catalytic activity of dihydrofolate reductase from the hyperthermophile Thermotoga maritima (2009), Biochemistry, 48, 5922-5933 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| V11D | the single amino acid replacement is sufficient to favor the monomeric form of the enzyme in the presence of the nondenaturing zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate. The free energy of stabilization of monomeric mutant enzyme V11D is 15 kJ/mol lower than that of the wild-type dimer. Both the steady-state turnover numbers and rates of hydride transfer are reduced in V11D | Thermotoga maritima |
| V126E | mutant enzyme remains as a dimer, steady-state turnover numbers and rates of hydride transfer are reduced | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | Q60034 | - |
- |
| Thermotoga maritima DSM 3109 | Q60034 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermotoga maritima |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 7,8-dihydrofolate + NADPH + H+ | - |
Thermotoga maritima | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? |  |
| 7,8-dihydrofolate + NADPH + H+ | - |
Thermotoga maritima DSM 3109 | 5,6,7,8-tetrahydrofolate + NADP+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | - |
Thermotoga maritima |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DHFR | - |
Thermotoga maritima |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Thermotoga maritima |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the free energy of stabilization of monomeric mutant enzyme V11D is 15 kJ/mol lower than that of the wild-type dimer, while the melting temperature of monomeric mutant enzyme V11D is comparable to that of monomeric DHFR from the thermophile Bacillus stearothermophilus, supporting the hypothesis that oligomerization is required to achieve the thermal stabilities necessary for activity at temperatures optimal for growth of hyperthermophiles | Thermotoga maritima |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Thermotoga maritima |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | - |
Thermotoga maritima | |
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Release 2023.1 (January 2023)
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