Using enzyme promiscuity to develop new biocatalysts is especially attractive for abiological reactions and can contribute to expanding our knowledge of the parameters involved in natural and laboratory enzyme evolution. A fascinating example of a catalytically promiscuous enzyme is 4-oxalocrotonate tautomerase (4-OT) from Pseudomonas putida mt-2, which utilizes an amino-terminal proline as key catalytic residue to promiscuously catalyze C-C bond-forming reactions, such as Michael additions and aldol condensations. The aim of the work described in this thesis was to further explore 4-OT for different synthetically useful C-C bond-forming reactions, as well as to improve its biocatalytic properties by mutability-landscape-guided protein engineering.
|Kwalificatie||Doctor of Philosophy|
|Datum van toekenning||12-mrt-2021|
|Plaats van publicatie||[Groningen]|
|Status||Published - 2021|