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Literature summary 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

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

General Stability

EC Number General Stability Organism
2.1.1.63 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

EC Number Organic Solvent Comment Organism
2.1.1.63 2,2,2-trifluoroethanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
2.1.1.63 2-propanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
2.1.1.63 Ethanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
2.1.1.63 Methanol enzyme retains its native structure at high concentrations Thermococcus kodakarensis
2.1.1.63 SDS enzyme retains its native structure at high concentrations Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.63 Thermococcus kodakarensis
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-
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Synonyms

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