ArticleMicrobial cell factories2026
Engineering Pseudomonas taiwanensis VLB120 for regio- and stereospecific hydroxylation of L-lysine fueled by the Weimberg pathway.
Article in Microbial cell factories, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundHydroxy-L-lysines are versatile chiral building blocks and can be obtained by hydroxylation of the amino acid L-lysine. The conversion is catalyzed by α-ketoglutarate-dependent lysine dioxygenases (KDOs), which belong to the superfamily of Fe
resultsFor the generation of a suitable whole-cell biocatalyst, we investigated the L-lysine catabolism of P. taiwanensis VLB120 and created a mutant strain that is deficient in L-lysine catabolism to minimize L-lysine degradation and to facilitate complete conversion via the biotransformation reaction. Next, a library of KDO genes was heterologously expressed in the engineered chassis strain P. taiwanensis VLB120∆C∆3. The hydroxylation of L-lysine was assessed in biotransformations with growing cells and D-xylose to supply α-KG via the Weimberg pathway. Hydroxy-L-lysine was successfully produced by strains harboring KDOs that hydroxylate the C-4 position of L-lysine. We further explored the three most promising whole-cell biocatalysts and investigated the influence of increased concentrations of the substrate L-lysine and the metal cofactor Fe
conclusionsWe successfully established a whole-cell biocatalyst for the synthesis of hydroxy-L-lysine from L-lysine and D-xylose and demonstrated multigram-scale production with our engineered strain. Our work lays the foundation for whole-cell bioprocesses utilizing Fe
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