Photocontrolling the Enantioselectivity of a Phosphotriesterase via Incorporation of a Light-Responsive Unnatural Amino Acid.

ABSTRACT: The external control of catalytic activity and substrate specificity of enzymes by light has aroused great interest in the fields of biocatalysis and pharmacology. Going beyond, we have attempted to photocontrol enzyme stereoselectivity on the example of phosphotriesterase (PTE), which is capable of hydrolyzing a wide variety of racemic organophosphorus substrates where one of two enantiomers is often highly toxic. To pursue this goal, the photocaged unnatural amino acid o-nitrobenzyl-l-tyrosine (ONBY) was incorporated by genetic code expansion at the large subsite of the active center, together with additional mutations at the small subsite. The stereoselectivities of the resulting PTE variants were tested with the achiral control substrate paraoxon and four different racemic subst

SUBMITTER: Hiefinger C 

PROVIDER: S-EPMC11863162 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature