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Literature summary for 2.1.1.63 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)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
E93A mutant enzyme unfolds one order of magnitude faster than does the wild-type enzyme Thermococcus kodakarensis

Organic Solvent Stability

Organic Solvent Comment Organism
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

Organism UniProt Comment Textmining
Thermococcus kodakarensis
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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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
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-
Thermococcus kodakarensis