Effect of surface electrostatic interactions on the stability and folding of formate dehydrogenase from Candida methylica

- kcat/Km of Q105R is equal to native cmFDH and this mutant increase the T0.5 value as 6 °C.
- Y160E has higher kcat/Km (0.35 s−1 mM−1) than that of native (0.24 s−1 mM−1).
- The Tm value was increased nearly 3 °C for N147R and Q105.
- The most significant increase in Tm was observed for the N187E as 6 °C.
- H13E, Y160E, Y160R and Y302R showed on average of 6 kcal/mol destabilizing effect.