Engineered Proline-based Carboligases With Improved Catalytic Properties

Chao Guo

Onderzoeksoutput: Thesis fully internal (DIV)

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Samenvatting

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.
Originele taal-2English
KwalificatieDoctor of Philosophy
Toekennende instantie
  • Rijksuniversiteit Groningen
Begeleider(s)/adviseur
  • Poelarends, Gerrit, Supervisor
  • Quax, W. J., Supervisor
Datum van toekenning12-mrt-2021
Plaats van publicatie[Groningen]
Uitgever
DOI's
StatusPublished - 2021

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