Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro

Andreas Stahl Madsen; Christian Adam Olsen

doi:10.1002/anie.201203754

Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro

Andreas Stahl Madsen, Christian Adam Olsen

Department of Chemistry

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

Systematic screening of the activities of the eleven human zinc-dependent lysine deacylases against a series of fluorogenic substrates (see scheme) 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.

Original language	English
Journal	Angewandte Chemie International Edition
Volume	51
Issue number	36
Pages (from-to)	9083-9087
ISSN	1433-7851
DOIs	https://doi.org/10.1002/anie.201203754
Publication status	Published - 2012

Keywords

Enzymes
Epigenetics
Histone deacetylases
Inhibitors
Posttranslational modifications

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AB - Systematic screening of the activities of the eleven human zinc-dependent lysine deacylases against a series of fluorogenic substrates (see scheme) 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.

KW - Enzymes

KW - Epigenetics

KW - Histone deacetylases

KW - Inhibitors

KW - Posttranslational modifications

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M3 - Journal article

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ER -

Profiling of Substrates for Zinc‐dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro

Abstract

Keywords

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