Thermostabilization of firefly luciferase by a single amino acid substitution at position 217.

@article{Kajiyama1993ThermostabilizationOF,
  title={Thermostabilization of firefly luciferase by a single amino acid substitution at position 217.},
  author={Naoki Kajiyama and Eiichi Nakano},
  journal={Biochemistry},
  year={1993},
  volume={32 50},
  pages={13795-9}
}
Random mutagenesis of the luciferase cDNA from "Genji" firefly, Luciola cruciata, was induced by hydroxylamine in an attempt to isolate thermostable mutants. Three mutants were isolated, and the cDNAs encoding these proteins were sequenced. All mutant cDNAs carried the same C to T transition mutation that conferred an amino acid substitution of Thr by Ile at position 217. The wild-type luciferase and the thermostable variant (Thr217Ile) were purified to homogeneity, and their enzymatic… CONTINUE READING

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