Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits decrotonylase activity in vitro

Andreas S Madsen; Christian A Olsen

doi:10.1002/anie.201203754

Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits decrotonylase activity in vitro

Angew Chem Int Ed Engl. 2012 Sep 3;51(36):9083-7. doi: 10.1002/anie.201203754. Epub 2012 Aug 13.

Authors

Andreas S Madsen¹, Christian A Olsen

Affiliation

¹ Department of Chemistry, Technical University of Denmark, Kgs. Lyngby, 2800 Denmark.

PMID: 22890609
DOI: 10.1002/anie.201203754

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

HeLa Cells
Histone Deacetylase Inhibitors / chemistry
Histone Deacetylases / chemistry
Histone Deacetylases / metabolism*
Humans
Kinetics
Nuclear Receptor Co-Repressor 1 / chemistry
Nuclear Receptor Co-Repressor 1 / metabolism
Protein Isoforms / chemistry
Protein Isoforms / metabolism
Substrate Specificity
Zinc / chemistry*

Substances

Histone Deacetylase Inhibitors
Nuclear Receptor Co-Repressor 1
Protein Isoforms
Histone Deacetylases
histone deacetylase 3
Zinc