Is JmjC oxygenase catalysis limited to demethylation?
Jobs on the side: Substrate selectivity studies indicate that members of the biomedically important JmjC demethylase family of histone N(ε)-methyllysine demethylases are capable of catalyzing the de-N-alkylation of groups other than N-methyl and can catalyze reactions that form stable hydroxylated p...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2013
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| _version_ | 1826285555847004160 |
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| author | Hopkinson, R Walport, L Münzel, M Rose, N Smart, T Kawamura, A Claridge, T Schofield, C |
| author_facet | Hopkinson, R Walport, L Münzel, M Rose, N Smart, T Kawamura, A Claridge, T Schofield, C |
| author_sort | Hopkinson, R |
| collection | OXFORD |
| description | Jobs on the side: Substrate selectivity studies indicate that members of the biomedically important JmjC demethylase family of histone N(ε)-methyllysine demethylases are capable of catalyzing the de-N-alkylation of groups other than N-methyl and can catalyze reactions that form stable hydroxylated products. The differences in binding preferences in this set of enzymes may be helpful in the design of selective inhibitors. |
| first_indexed | 2024-03-07T01:30:35Z |
| format | Journal article |
| id | oxford-uuid:9377f90f-c0f6-46b5-8111-680eef22d835 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:30:35Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | oxford-uuid:9377f90f-c0f6-46b5-8111-680eef22d8352022-03-26T23:32:29ZIs JmjC oxygenase catalysis limited to demethylation?Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:9377f90f-c0f6-46b5-8111-680eef22d835EnglishSymplectic Elements at Oxford2013Hopkinson, RWalport, LMünzel, MRose, NSmart, TKawamura, AClaridge, TSchofield, CJobs on the side: Substrate selectivity studies indicate that members of the biomedically important JmjC demethylase family of histone N(ε)-methyllysine demethylases are capable of catalyzing the de-N-alkylation of groups other than N-methyl and can catalyze reactions that form stable hydroxylated products. The differences in binding preferences in this set of enzymes may be helpful in the design of selective inhibitors. |
| spellingShingle | Hopkinson, R Walport, L Münzel, M Rose, N Smart, T Kawamura, A Claridge, T Schofield, C Is JmjC oxygenase catalysis limited to demethylation? |
| title | Is JmjC oxygenase catalysis limited to demethylation? |
| title_full | Is JmjC oxygenase catalysis limited to demethylation? |
| title_fullStr | Is JmjC oxygenase catalysis limited to demethylation? |
| title_full_unstemmed | Is JmjC oxygenase catalysis limited to demethylation? |
| title_short | Is JmjC oxygenase catalysis limited to demethylation? |
| title_sort | is jmjc oxygenase catalysis limited to demethylation |
| work_keys_str_mv | AT hopkinsonr isjmjcoxygenasecatalysislimitedtodemethylation AT walportl isjmjcoxygenasecatalysislimitedtodemethylation AT munzelm isjmjcoxygenasecatalysislimitedtodemethylation AT rosen isjmjcoxygenasecatalysislimitedtodemethylation AT smartt isjmjcoxygenasecatalysislimitedtodemethylation AT kawamuraa isjmjcoxygenasecatalysislimitedtodemethylation AT claridget isjmjcoxygenasecatalysislimitedtodemethylation AT schofieldc isjmjcoxygenasecatalysislimitedtodemethylation |