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Literature summary for 2.1.1.63 extracted from

  • Nishikori, S.; Shiraki, K.; Okanojo, M.; Imanaka, T.; Takagi, M.
    Equilibrium and kinetic stability of a hyperthermophilic protein, O6-methylguanine-DNA methyltransferase under various extreme conditions (2004), J. Biochem., 136, 503-508.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E93A stability against organic solvents does not differ from that of the wild-type enzyme Thermococcus kodakarensis

General Stability

General Stability Organism
guanidine-HCl, half-time for unfolding at 30°C is 52 days. An ion-pair network plays a key role in the slow unfolding Thermococcus kodakarensis

Organic Solvent Stability

Organic Solvent Comment Organism
2,2,2-trifluoroethanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
2-propanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
Ethanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
Methanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
SDS enzyme retains its native structure at high concentrations Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis
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-
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Synonyms

Synonyms Comment Organism
O6-methylguanine-DNA methyltransferase
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Thermococcus kodakarensis
Tk-MGMT
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Thermococcus kodakarensis