Literature summary for 2.1.2.1 extracted from

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

Search for more literature for 2.1.2.1

Organism

Organism	UniProt	Comment	Textmining
Aeropyrum pernix	-	-	-
Aquifex aeolicus	-	-	-
Archaeoglobus fulgidus	-	-	-
Methanocaldococcus jannaschii	-	-	-
Methanothermobacter marburgensis	-	-	-
Methanothermobacter thermautotrophicus	-	-	-
Pyrococcus abyssi	-	-	-
Pyrococcus horikoshii	-	-	-
Saccharolobus solfataricus	-	-	-
Thermotoga maritima	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Ser + tetrahydrofolate	-	Methanothermobacter thermautotrophicus	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Saccharolobus solfataricus	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Methanocaldococcus jannaschii	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Archaeoglobus fulgidus	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Thermotoga maritima	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Pyrococcus horikoshii	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Aquifex aeolicus	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Aeropyrum pernix	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Pyrococcus abyssi	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?
L-Ser + tetrahydrofolate	-	Methanothermobacter marburgensis	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?

Synonyms

Synonyms	Comment	Organism
SHMT	-	Methanothermobacter thermautotrophicus
SHMT	-	Saccharolobus solfataricus
SHMT	-	Methanocaldococcus jannaschii
SHMT	-	Archaeoglobus fulgidus
SHMT	-	Thermotoga maritima
SHMT	-	Pyrococcus horikoshii
SHMT	-	Aquifex aeolicus
SHMT	-	Aeropyrum pernix
SHMT	-	Pyrococcus abyssi
SHMT	-	Methanothermobacter marburgensis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
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
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
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
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
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
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
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
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
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
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

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Release 2023.1 (January 2023)