Human histone demethylase KDM6B can catalyse sequential oxidations

Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of N(ε)-methylated lysines on histones and play important roles in gene regulation. We report selectivity studies on KDM6B (JMJD3), a disease-relevant JmjC-KDM, using synthetic lysine analogues. The results unexpectedly reveal...

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Autores principales: Hopkinson, Richard J., Langley, Gareth W., Belle, Roman, Walport, Louise J., Dunne, Kate, Münzel, Martin, Salah, Eidarus, Kawamura, Akane, Claridge, Timothy D. W., Schofield, Christopher J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6044289/
https://www.ncbi.nlm.nih.gov/pubmed/29961803
http://dx.doi.org/10.1039/c8cc04057e
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author Hopkinson, Richard J.
Langley, Gareth W.
Belle, Roman
Walport, Louise J.
Dunne, Kate
Münzel, Martin
Salah, Eidarus
Kawamura, Akane
Claridge, Timothy D. W.
Schofield, Christopher J.
author_facet Hopkinson, Richard J.
Langley, Gareth W.
Belle, Roman
Walport, Louise J.
Dunne, Kate
Münzel, Martin
Salah, Eidarus
Kawamura, Akane
Claridge, Timothy D. W.
Schofield, Christopher J.
author_sort Hopkinson, Richard J.
collection PubMed
description Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of N(ε)-methylated lysines on histones and play important roles in gene regulation. We report selectivity studies on KDM6B (JMJD3), a disease-relevant JmjC-KDM, using synthetic lysine analogues. The results unexpectedly reveal that KDM6B accepts multiple N(ε)-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products.
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spelling pubmed-60442892018-08-03 Human histone demethylase KDM6B can catalyse sequential oxidations Hopkinson, Richard J. Langley, Gareth W. Belle, Roman Walport, Louise J. Dunne, Kate Münzel, Martin Salah, Eidarus Kawamura, Akane Claridge, Timothy D. W. Schofield, Christopher J. Chem Commun (Camb) Chemistry Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of N(ε)-methylated lysines on histones and play important roles in gene regulation. We report selectivity studies on KDM6B (JMJD3), a disease-relevant JmjC-KDM, using synthetic lysine analogues. The results unexpectedly reveal that KDM6B accepts multiple N(ε)-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products. Royal Society of Chemistry 2018-07-21 2018-07-02 /pmc/articles/PMC6044289/ /pubmed/29961803 http://dx.doi.org/10.1039/c8cc04057e Text en This journal is © The Royal Society of Chemistry 2018 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Hopkinson, Richard J.
Langley, Gareth W.
Belle, Roman
Walport, Louise J.
Dunne, Kate
Münzel, Martin
Salah, Eidarus
Kawamura, Akane
Claridge, Timothy D. W.
Schofield, Christopher J.
Human histone demethylase KDM6B can catalyse sequential oxidations
title Human histone demethylase KDM6B can catalyse sequential oxidations
title_full Human histone demethylase KDM6B can catalyse sequential oxidations
title_fullStr Human histone demethylase KDM6B can catalyse sequential oxidations
title_full_unstemmed Human histone demethylase KDM6B can catalyse sequential oxidations
title_short Human histone demethylase KDM6B can catalyse sequential oxidations
title_sort human histone demethylase kdm6b can catalyse sequential oxidations
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6044289/
https://www.ncbi.nlm.nih.gov/pubmed/29961803
http://dx.doi.org/10.1039/c8cc04057e
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