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Literature summary extracted from

  • Nishikori, S.; Shiraki, K.; Yokota, K.; Izumikawa, N.; Fujiwara, S.; Hashimoto, H.; Imanaka, T.; Takagi, M.
    Mutational effects on O6-methylguanine-DNA methyltransferase from hyperthermophile: Contribution of ion-pair network to protein thermostability (2004), J. Biochem., 135, 525-532.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.63 recombinant variants are expressed in HMS174 pLyS cells Thermococcus kodakarensis

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.63 E158A melting temperature of mutant enzyme E83A at 5 mM urea is 90.6°C, compared to 91.5°C for the wild-type enzyme Thermococcus kodakarensis
2.1.1.63 E159A melting temperature of mutant enzyme E83A at 5 mM urea is 91.7°C, compared to 91.5°C for the wild-type enzyme Thermococcus kodakarensis
2.1.1.63 E83A melting temperature of mutant enzyme E83A at 5 mM urea is 89.2°C, compared to 91.5°C for the wild-type enzyme Thermococcus kodakarensis
2.1.1.63 E93A mutant enzyme unfolds one order of magnitude faster than does the wild-type enzyme Thermococcus kodakarensis

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
2.1.1.63 urea 5 mM, melting temperature of wild-type enzyme: 91.5 °C, melting temperature of mutant enzyme E83A: 89.2°C, melting temperature of mutant enzyme E93A: 85.5°C, melting temperature of mutant enzyme E158A: 90.6°C, melting temperature of mutant enzyme E159A: 91.7 °C Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.63 Thermococcus kodakarensis
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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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.63 50
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 Thermococcus kodakarensis