Design of a novel catalytic function in proteins and peptides, apart from its inherent practical value, is important for fundamental understanding of enzymatic activity. We will present applications of a computationally inexpensive, minimalistic approach to design of artificial enzymes. This method allows for in silico pre-screening of many possible protein variants at a very low cost. Introducing single amino acid residue mutations into a 74-residue-long C-terminal domain of calmodulin confers catalytic activities (Kemp elimination, ester hydrolysis, retroaldol reaction) onto this non-enzymatic protein. The catalytic efficiencies of the resulting allosterically regulated catalysts are on par with those of the best computational approaches. Directed evolution allowed for further improvement of catalysts' efficiency.

Computational design and directed evolution of allosterically regulated enzymes

249th National Meeting (2015)

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