Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation
The JmjC histone demethylases (KDMs) play important roles in modulating histone methylation states and have the potential to be regulated by oxygen availability. Lys-241 of the KDM4 subfamily is proposed to be important in oxygen binding by KDM4A. We report evidence that, although K241 is unlikely t...
| 主要な著者: | , , , , , , |
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| フォーマット: | Journal article |
| 言語: | English |
| 出版事項: |
Wiley‐VCH Verlag
2018
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| _version_ | 1826302317458096128 |
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| author | Hancock, R Abboud, M Smart, T Flashman, E Kawamura, A Schofield, C Hopkinson, R |
| author_facet | Hancock, R Abboud, M Smart, T Flashman, E Kawamura, A Schofield, C Hopkinson, R |
| author_sort | Hancock, R |
| collection | OXFORD |
| description | The JmjC histone demethylases (KDMs) play important roles in modulating histone methylation states and have the potential to be regulated by oxygen availability. Lys-241 of the KDM4 subfamily is proposed to be important in oxygen binding by KDM4A. We report evidence that, although K241 is unlikely to be directly involved in oxygen binding, it has an important role in coupling 2-oxoglutarate cosubstrate oxidation with lysine demethylase activity. The results suggest that compounds promoting uncoupling of substrate oxidation are of interest as JmjC-KDM inhibitors. |
| first_indexed | 2024-03-07T05:45:44Z |
| format | Journal article |
| id | oxford-uuid:e72718d3-2267-4420-91e0-977e57bc12c6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:45:44Z |
| publishDate | 2018 |
| publisher | Wiley‐VCH Verlag |
| record_format | dspace |
| spelling | oxford-uuid:e72718d3-2267-4420-91e0-977e57bc12c62022-03-27T10:36:31ZLysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylationJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e72718d3-2267-4420-91e0-977e57bc12c6EnglishSymplectic Elements at OxfordWiley‐VCH Verlag2018Hancock, RAbboud, MSmart, TFlashman, EKawamura, ASchofield, CHopkinson, RThe JmjC histone demethylases (KDMs) play important roles in modulating histone methylation states and have the potential to be regulated by oxygen availability. Lys-241 of the KDM4 subfamily is proposed to be important in oxygen binding by KDM4A. We report evidence that, although K241 is unlikely to be directly involved in oxygen binding, it has an important role in coupling 2-oxoglutarate cosubstrate oxidation with lysine demethylase activity. The results suggest that compounds promoting uncoupling of substrate oxidation are of interest as JmjC-KDM inhibitors. |
| spellingShingle | Hancock, R Abboud, M Smart, T Flashman, E Kawamura, A Schofield, C Hopkinson, R Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation |
| title | Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation |
| title_full | Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation |
| title_fullStr | Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation |
| title_full_unstemmed | Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation |
| title_short | Lysine-241 has a role in coupling 2OG turnover with substrate oxidation during KDM4-catalysed histone demethylation |
| title_sort | lysine 241 has a role in coupling 2og turnover with substrate oxidation during kdm4 catalysed histone demethylation |
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