PadR-based artificial enzymes
| PhD ceremony: | B. Brouwer, MSc |
| When: | September 08, 2025 |
| Start: | 11:00 |
| Supervisors: | prof. dr. J.G. (Gerard) Roelfes, S. (Syuzanna) Harutyunyan, Prof |
| Where: | Academy building RUG |
| Faculty: | Science and Engineering |
In his thesis, Bart Brouwer describes the development of new building blocks and protein structures for the creation of artificial enzymes. By introducing a noncanonical amino acid, 3-aminotyrosine, into proteins using genetic techniques, Brouwer produced artificial enzymes that can carry out specific chemical reactions efficiently and selectively. This noncanonical amino acid can be easily incorporated into proteins and offers additional possibilities for designing enzymes with new functions.
Furthermore, through computer analyses and experiments, Brouwer discovered new proteins from the PadR family, from which also the versatile LmrR protein originates, and can serve as a basis for the creation of future artificial enzymes. Brouwer also created modified LmrR proteins, consisting of a single amino acid chain, making it easier to alter their properties and adapt them for various applications.
The work presented in this thesis has significantly expanded the repertoire of proteins and catalytic noncanonical amino acids available for creating artificial enzymes. The tools and insights presented offer new opportunities for designing future artificial enzymes with desired properties, thereby bringing the synthetic application of these enzymes closer to reality.