Human histone demethylase KDM6B can catalyse sequential oxidations
Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of Nε-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 t...
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
Royal Society of Chemistry
2018
|
| _version_ | 1797084771596107776 |
|---|---|
| author | Hopkinson, R Langley, G Belle, R Walport, L Dunne, K Münzel, M Salah, E Kawamura, A Claridge, T Schofield, C |
| author_facet | Hopkinson, R Langley, G Belle, R Walport, L Dunne, K Münzel, M Salah, E Kawamura, A Claridge, T Schofield, C |
| author_sort | Hopkinson, R |
| collection | OXFORD |
| description | Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of Nε-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 Nε-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products. |
| first_indexed | 2024-03-07T01:59:42Z |
| format | Journal article |
| id | oxford-uuid:9cea0a11-383d-4a34-9b2f-9638240ee449 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:59:42Z |
| publishDate | 2018 |
| publisher | Royal Society of Chemistry |
| record_format | dspace |
| spelling | oxford-uuid:9cea0a11-383d-4a34-9b2f-9638240ee4492022-03-27T00:39:35ZHuman histone demethylase KDM6B can catalyse sequential oxidationsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9cea0a11-383d-4a34-9b2f-9638240ee449EnglishSymplectic Elements at OxfordRoyal Society of Chemistry2018Hopkinson, RLangley, GBelle, RWalport, LDunne, KMünzel, MSalah, EKawamura, AClaridge, TSchofield, CJumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of Nε-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 Nε-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products. |
| spellingShingle | Hopkinson, R Langley, G Belle, R Walport, L Dunne, K Münzel, M Salah, E Kawamura, A Claridge, T Schofield, C 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 |
| work_keys_str_mv | AT hopkinsonr humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT langleyg humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT beller humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT walportl humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT dunnek humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT munzelm humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT salahe humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT kawamuraa humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT claridget humanhistonedemethylasekdm6bcancatalysesequentialoxidations AT schofieldc humanhistonedemethylasekdm6bcancatalysesequentialoxidations |