Enzymes are widely used in industry and his improvement by protein engineering is a growing field. Mutations in active site environment for activity improvement have proved to be highly successful1, but the possibility to create an enzyme with more than one catalytic site remains unexplored. Applying computational-aided rational design, we engineered a new esterase with two fully functional catalytic triads. By using Protein Energy Landscape Exploration software, we found non-catalytic binding sites capable of holding an active site and turning them to catalytic by mutagenesis. The result was the production of a new esterase with two reaction points instead of one. This finding opens a door of new opportunities on enzyme engineering.