Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues
| Autor: | Steven D. Bull, Kazuya Kikuchi, Miyako Nishiura, Reisuke Baba, Yuichiro Hori, Tomomi Tao |
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| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Enzyme catalyzed Lysine Peptide General Chemistry 010402 general chemistry 01 natural sciences Fluorescence 0104 chemical sciences Turn (biochemistry) 03 medical and health sciences Chemistry Enzyme chemistry Biochemistry Demethylase activity 030304 developmental biology |
| Zdroj: | Chemical Science |
| ISSN: | 2041-6520 |
| Popis: | Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneous O- to N-ester transfer reactions (uncatalyzed) to generate a highly fluorescent N-carbamoyl peptide. This enables detection of enzyme catalyzed N-deacetylation, N-demalonylation, N-desuccinylation and N-demethylation reactions activities towards the N-modified lysine residues of these probes using simple ‘turn on’ fluorescent assays. We developed “turn-on” fluorescent probes that detect enzymatic lysine deacylation and demethylation critical for epigenetic and other cellular phenomena, using intramolecular O- to N-ester transfer reactions. |
| Databáze: | OpenAIRE |
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