Editing Thermostable Luciferase (section)

=== P.pyralis luciferase ===

These substitutions ('''F16R, L37Q, V183K, I234K and F465R''') led to the enzyme with greatly improved pH-tolerance and stability up to 45°C. The mutant showed neither a decrease in specific activity relative to the wild-type luciferase (Law et al., 2006). Introduction of almost all known point mutations (12 residues) enhancing the thermostability of P. pyralis luciferase resulted in a highly stable mutant with half-time of inactivation of 15 min at 55°C, whereas wild-type luciferase inactivates within seconds at this conditions (Tisi et al., 2007)