ArticleChembiochem : a European journal of chemical biology2022
Controlling Enzymatic Activity by Modulating the Oligomerization State via Chemical Rescue and Optical Control.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Modulation of succinyl-CoA:3-ketoacid CoA transferase activity by a single amino acid residue in acetate:succinate CoA transferase from Trypanosoma brucei, the causative agent of African sleeping sickness.Protein science : a publication of the Protein Society · 2026Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Photocontrolling the Enantioselectivity of a Phosphotriesterase via Incorporation of a Light-Responsive Unnatural Amino Acid.JACS Au · 2025Article
- Controlling Enzymatic Activity by Modulating the Oligomerization State via Chemical Rescue and Optical Control.Chembiochem : a European journal of chemical biology · 2022Article
- Biochemical and functional characterization ofFrontiers in microbiology · 2022Article
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Authors and funding
3 authors.
Funding
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Abstract
Selective switching of enzymatic activity has been a longstanding goal in synthetic biology. Drastic changes in activity upon mutational manipulation of the oligomerization state of enzymes have frequently been reported in the literature, but scarcely exploited for switching. Using geranylgeranylglyceryl phosphate synthase as a model, we demonstrate that catalytic activity can be efficiently controlled by exogenous modulation of the association state. We introduced a lysine-to-cysteine mutation, leading to the breakdown of the active hexamer into dimers with impaired catalytic efficiency. Addition of bromoethylamine chemically rescued the enzyme by restoring hexamerization and activity. As an alternative method, we incorporated the photosensitive unnatural amino acid o-nitrobenzyl-O-tyrosine (ONBY) into the hexamerization interface. This again led to inactive dimers, but the hexameric state and activity could be recovered by UV-light induced cleavage of ONBY. For both approaches, we obtained switching factors greater than 350-fold, which compares favorably with previously reported activity changes that were caused by site-directed mutagenesis.
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Registered trials
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