Enzyme engineering for optimizing biosynthesis of 2,4-dihydroxybutyric acid via the synthetic threose-dependent glycolaldehyde assimilation (STEGA) pathway
) on D-threose compared to the wild-type enzyme. As a consequence of these improvements, co-expression of both engineered enzymes in the STEGA pathway significantly enhanced EG-to-DHB bioconversion, achieving a 68% increase in final DHB titer (5.2 ± 0.11 mM) and a 23% improvement in carbon yield (0.16 ± 0.003 Cmol/Cmol).
Authors
- Linxuan Wen
- Thomas Walther
- Johannes Radde
- Cláudio J.R. Frazão
- Alrik Titze
- Christopher M. Topham
Institutions
- Technische Universität Dresden (DE)
Publication Details
- Journal
- Metabolic Engineering
- Published
- 2026-04-14
- DOI
- https://doi.org/10.1016/j.ymben.2026.04.005
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- European Commission
- Deutsche Forschungsgemeinschaft