Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits decrotonylase activity in vitro.
AS Madsen, CA Olsen - Angewandte Chemie (International ed. in …, 2012 - europepmc.org
AS Madsen, CA Olsen
Angewandte Chemie (International ed. in English), 2012•europepmc.orgSystematic screening of the activities of the eleven human zinc-dependent lysine
deacylases against a series of fluorogenic substrates as well as kinetic evaluation revealed
substrates for screenings of histone deacetylases HDAC10 and HDAC11 at reasonably low
enzyme concentrations. Furthermore, HDAC3 in complex with nuclear receptor corepressor
1 (HDAC3-NCoR1) was shown to harbor decrotonylase activity in vitro.
deacylases against a series of fluorogenic substrates as well as kinetic evaluation revealed
substrates for screenings of histone deacetylases HDAC10 and HDAC11 at reasonably low
enzyme concentrations. Furthermore, HDAC3 in complex with nuclear receptor corepressor
1 (HDAC3-NCoR1) was shown to harbor decrotonylase activity in vitro.
Systematic screening of the activities of the eleven human zinc-dependent lysine deacylases against a series of fluorogenic substrates as well as kinetic evaluation revealed substrates for screenings of histone deacetylases HDAC10 and HDAC11 at reasonably low enzyme concentrations. Furthermore, HDAC3 in complex with nuclear receptor corepressor 1 (HDAC3-NCoR1) was shown to harbor decrotonylase activity in vitro.
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