2.1.2.1: glycine hydroxymethyltransferase
This is an abbreviated version!
For detailed information about glycine hydroxymethyltransferase, go to the full flat file.
Word Map on EC 2.1.2.1
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2.1.2.1
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one-carbon
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pyridoxal
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thymidylate
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purine
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5'-phosphate
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homocysteine
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dihydrofolate
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folate-dependent
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photorespiratory
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photorespiration
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folate-mediated
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pyridoxal-5'-phosphate
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thf
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dtmp
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mthfd1
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plp-dependent
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remethylation
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aldimine
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phgdh
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medicine
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folate-metabolizing
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5,10-methenyltetrahydrofolate
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5'-phosphate-dependent
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antifolate
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hydroxypyruvate
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quinonoid
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5-methyltetrahydrofolate
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glycerate
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5-formyltetrahydrofolate
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drug development
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folate-related
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d-alanine
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c1-tetrahydrofolate
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1-carbon
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5-formyl
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polyglutamate
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l-threonine
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alpha-protons
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slc19a1
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retro-aldol
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degradation
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analysis
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synthesis
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biotechnology
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pharmacology
- 2.1.2.1
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one-carbon
- pyridoxal
- thymidylate
- purine
- 5'-phosphate
- homocysteine
- dihydrofolate
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folate-dependent
-
photorespiratory
-
photorespiration
-
folate-mediated
- pyridoxal-5'-phosphate
- thf
- dtmp
- mthfd1
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plp-dependent
-
remethylation
-
aldimine
- phgdh
- medicine
-
folate-metabolizing
- 5,10-methenyltetrahydrofolate
-
5'-phosphate-dependent
- antifolate
- hydroxypyruvate
-
quinonoid
- 5-methyltetrahydrofolate
- glycerate
- 5-formyltetrahydrofolate
- drug development
-
folate-related
- d-alanine
-
c1-tetrahydrofolate
-
1-carbon
-
5-formyl
- polyglutamate
- l-threonine
-
alpha-protons
-
slc19a1
-
retro-aldol
- degradation
- analysis
- synthesis
- biotechnology
- pharmacology
Reaction
Synonyms
AtSHMT3, bsSHMT, bstSHMT, EC 4.1.2.6, eSHMT, GlyA, GlyA protein, glycine hydroxymethyltransferrase, hSHMT, L-serine hydroxymethyltransferase, mitochondrial serine hydroxymethyltransferase, MJ1597, PvSHMT, Rhg4, serine hydroxymethyl transferase, serine hydroxymethylase hydroxymethyltransferase, serine, serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, serine hydroxymethyltransferase 2, serine hydroxymethyltransferase 2alpha, serine transhydroxymethylase, serine:H4F hydroxymethyltransferase, serine:tetrahydrofolate hydroxymethyltransferase, SHM1, SHM2, SHMT, SHMT-1, SHMT-L, SHMT-S, SHMT08, SHMT1, SHMT2, SHMT2alpha, SHMT3, zcSHMT, zebrafish cytosolic serine hydroxymethyltransferase, zebrafish mitochondiral serine hydroxymethyltransferase, zmSHMT
ECTree
2.1.2.1 glycine hydroxymethyltransferaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 2.1.2.1 - glycine hydroxymethyltransferase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
20 - 40
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the enzyme retains more than 80% of its activity after 30 min at 20-40°C. After 30 min at 45-50°C, the enzyme shows about 30% residual activity. The enzyme shows about 30% activity after 30 min at pH 10-12
30 - 65
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a broad sigmoidal transition between 30°C and 65°C having an apparent Tm of about 48°C is observed for the native dimeric SHMT molecule, SHMT is a noncooperative molecule which starts losing the structure from very low temperature (30°C) and loses most of ist secondary structure at relatively high temperature
35 - 55
after 1 h incubation under pH 7.5, the enzyme retains over 35% of its maximal activity from 35°C to 45°C, but less than 15% at 55°C
40
45 - 65
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the wild type enzyme shows a rapid decrease (to less than 20%) in activity after 30 min at 55-65°C, and shows about 35% activity after 30 min at 45°C
55
60
65
70
additional information
40
the enzyme retains over 45% of its maximal activity after incubation at 40°C for 3 h
55
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Tm-value for wild-type enzyme and mutant enzymes R262A, S52C and S52A without ligands or with Gly as ligand. Tm-value for mutant enzymes mutant enzymes R262A, S52C and S52A with L-Ser as ligand
60
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for 10 min, the native enzyme conserves about 40% of its activity, while the mutant 3E7 retains about 56% of its activity
65
the melting temperature of the wild type enzyme is at 65°C
70
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complete loss of activity after 6 min, enzyme-antibody complex: 30% loss of activity after 20 min
additional information
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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
additional information
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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
additional information
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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
additional information
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Tm values of enzyme and dimeric and tetrameric forms in the absence and presence of ligands
additional information
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pyridoxal 5'-phosphate increases the thermal stability
additional information
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L-serine increases the thermal stability
additional information
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enzyme-antibody complex more stable to elevated temperatures than free enzyme, allosteric effectors fail to protect free enzyme
additional information
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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
additional information
the crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
additional information
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the crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures
additional information
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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
additional information
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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
additional information
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Tm: 55°C, increased to 65°C in the presence of L-serine, Tm: 68°C mutant enzyme Y82F in the presence of serine
additional information
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Tm of wild-type and mutant enzyme: 54°C, in the presence of serine Tm of wild-type enzyme: 63°C
additional information
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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
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
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
additional information
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glycerol, 30% v/v, enhances thermal stability
additional information
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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
