ArticleProceedings of the National Academy of Sciences of the United States of America2010
Controlling the enzymatic activity of a restriction enzyme by light.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 176 citations in OpenAlex.
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- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
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- Photoresponsive peptide materials: Spatiotemporal control of self-assembly and biological functions.Biophysics reviews · 2023Review
- Helicase Activity Modulation with On-Demand Light-Based Conformational Control.Journal of the American Chemical Society · 2023Article
- Cystine Knot Peptides with Tuneable Activity and Mechanism.Angewandte Chemie (International ed. in English) · 2022Article
- A simple and general approach to generate photoactivatable DNA processing enzymes.Nucleic acids research · 2022Article
- Using azobenzene photocontrol to set proteins in motion.Nature reviews. Chemistry · 2022Review
- Computational design and experimental characterization of a photo-controlled mRNA-cap guanine-N7 methyltransferase.RSC chemical biology · 2021Article
- Sensing the allosteric force.Nature communications · 2020Article
- Enzyme dynamics: Looking beyond a single structure.ChemCatChem · 2020Article
- Light Regulation of Two New Manganese Peroxidase-Encoding Genes inMicroorganisms · 2020Article
- Off-on switching of enzyme activity by near-infrared light-induced photothermal phase transition of nanohybrids.Science advances · 2019Article
- Stimulus-Responsive Regulation of Enzyme Activity for One-Step and Multi-Step Syntheses.Advanced synthesis & catalysis · 2019Review
- In search of visible-light photoresponsive peptide nucleic acids (PNAs) for reversible control of DNA hybridization.Beilstein journal of organic chemistry · 2019Article
- Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019Review
- Reversible and Tunable Photoswitching of Protein Function through Genetic Encoding of Azobenzene Amino Acids in Mammalian Cells.Chembiochem : a European journal of chemical biology · 2018Article
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For many applications it would be desirable to be able to control the activity of proteins by using an external signal. In the present study, we have explored the possibility of modulating the activity of a restriction enzyme with light. By cross-linking two suitably located cysteine residues with a bifunctional azobenzene derivative, which can adopt a cis- or trans-configuration when illuminated by UV or blue light, respectively, enzymatic activity can be controlled in a reversible manner. To determine which residues when cross-linked show the largest "photoswitch effect," i.e., difference in activity when illuminated with UV vs. blue light, > 30 variants of a single-chain version of the restriction endonuclease PvuII were produced, modified with azobenzene, and tested for DNA cleavage activity. In general, introducing single cross-links in the enzyme leads to only small effects, whereas with multiple cross-links and additional mutations larger effects are observed. Some of the modified variants, which carry the cross-links close to the catalytic center, can be modulated in their DNA cleavage activity by a factor of up to 16 by illumination with UV (azobenzene in cis) and blue light (azobenzene in trans), respectively. The change in activity is achieved in seconds, is fully reversible, and, in the case analyzed, is due to a change in V(max) rather than K(m).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.