One-Atom Substitution Enables Direct and Continuous Monitoring of Histone Deacylase Activity
| Autor: | Christophe Romier, Matthes Zessin, Martin Marek, Zsofia Kutil, Marat Meleshin, Zora Novakova, Wolfgang Sippl, Cyril Bařinka, Diana Kalbas, Mike Schutkowski, Ehab Ghazy |
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| Přispěvatelé: | Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institute of Pharmaceutical Chemistry, Martin-Luther-Universität Halle Wittenberg (MLU) |
| Rok vydání: | 2019 |
| Předmět: |
Stereochemistry
Lysine chemistry.chemical_element 010402 general chemistry 01 natural sciences Biochemistry Oxygen Histone Deacetylases 03 medical and health sciences Atom Humans Moiety [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences biology Chemistry Substitution (logic) Sulfur 0104 chemical sciences Histone Deacetylase Inhibitors Thioamides Kinetics Histone Direct assay Biocatalysis biology.protein |
| Zdroj: | Biochemistry Biochemistry, American Chemical Society, 2019, 58 (48), pp.4777-4789. ⟨10.1021/acs.biochem.9b00786⟩ |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/acs.biochem.9b00786 |
| Popis: | We developed a one-step direct assay for the determination of histone deacylase (HDAC) activity by substituting the carbonyl oxygen of the acyl moiety with sulfur, resulting in thioacylated lysine side chains. This modification is recognized by class I HDACs with different efficiencies ranging from not accepted for HDAC1 to kinetic constants similar to that of the parent oxo substrate for HDAC8. Class II HDACs can hydrolyze thioacylated substrates with approximately 5-10-fold reduced |
| Databáze: | OpenAIRE |
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