EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.2.1 | Aeropyrum pernix | - |
- |
- |
2.1.2.1 | Aquifex aeolicus | - |
- |
- |
2.1.2.1 | Archaeoglobus fulgidus | - |
- |
- |
2.1.2.1 | Methanocaldococcus jannaschii | - |
- |
- |
2.1.2.1 | Methanothermobacter marburgensis | - |
- |
- |
2.1.2.1 | Methanothermobacter thermautotrophicus | - |
- |
- |
2.1.2.1 | Pyrococcus abyssi | - |
- |
- |
2.1.2.1 | Pyrococcus horikoshii | - |
- |
- |
2.1.2.1 | Saccharolobus solfataricus | - |
- |
- |
2.1.2.1 | Thermotoga maritima | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Methanothermobacter thermautotrophicus | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Saccharolobus solfataricus | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Methanocaldococcus jannaschii | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Archaeoglobus fulgidus | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Thermotoga maritima | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Pyrococcus horikoshii | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Aquifex aeolicus | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Aeropyrum pernix | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Pyrococcus abyssi | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? | |
2.1.2.1 | L-Ser + tetrahydrofolate | - |
Methanothermobacter marburgensis | glycine + 5,10-methylenetetrahydrofolate + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.2.1 | SHMT | - |
Methanothermobacter thermautotrophicus |
2.1.2.1 | SHMT | - |
Saccharolobus solfataricus |
2.1.2.1 | SHMT | - |
Methanocaldococcus jannaschii |
2.1.2.1 | SHMT | - |
Archaeoglobus fulgidus |
2.1.2.1 | SHMT | - |
Thermotoga maritima |
2.1.2.1 | SHMT | - |
Pyrococcus horikoshii |
2.1.2.1 | SHMT | - |
Aquifex aeolicus |
2.1.2.1 | SHMT | - |
Aeropyrum pernix |
2.1.2.1 | SHMT | - |
Pyrococcus abyssi |
2.1.2.1 | SHMT | - |
Methanothermobacter marburgensis |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Methanothermobacter thermautotrophicus |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Saccharolobus solfataricus |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Methanocaldococcus jannaschii |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Archaeoglobus fulgidus |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Thermotoga maritima |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Pyrococcus horikoshii |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Aquifex aeolicus |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Aeropyrum pernix |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Pyrococcus abyssi |
2.1.2.1 | additional information | - |
thermophilic enzyme. Thermal stability of SHMT can be achieved mainly through three strategies: 1. increased number of charged residues at the protein surface, 2. increased hydrophobicity of the protein core, and 3. substitution of thermolabile residues exposed to the solvent | Methanothermobacter marburgensis |