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Literature summary extracted from

  • Paiardini, A.; Gianese, G.; Bossa, F.; Pascarella, S.
    Structural plasticity of thermophilic serine hydroxymethyltransferases (2003), Proteins, 50, 122-134.
    View publication on PubMed

Organism

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
-
-
-

Substrates and Products (Substrate)

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
-
 ?

Synonyms

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

Temperature Stability [°C]

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