Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits 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.
Department of Chemistry, Technical University of Denmark, Kgs. Lyngby, 2800 Denmark.
Andreas S
AS
Madsen
Christian A
CA
Olsen
D006367:HeLa Cells; D056572:Histone Deacetylase Inhibitors / Q000737:chemistry; D006655:Histone Deacetylases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D056971:Nuclear Receptor Co-Repressor 1 / Q000737:chemistry / Q000378:metabolism; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D015032:Zinc / Q000737:chemistry*; D000099186:Histone Deacetylase 3
D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases; D056971:Nuclear Receptor Co-Repressor 1; D020033:Protein Isoforms; D015032:Zinc; D000099186:Histone Deacetylase 3