Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation

The tolerance of a natural thermostable chorismate mutase and an engineered molten globular variant to targeted mutation is compared to understand the mutational robustness of homologous enzymes that correlates with a higher initial free energy of unfolding ([DELTA]G). The mutases are found to have similar sequence, structure, and catalytic efficiency but different [DELTA]G values and the analogous point mutations could have widely divergent effects on catalytic activity in the scaffolds.