Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases
The Jumonji-C (JmjC) subfamily of 2-oxoglutarate (2OG)-dependent oxygenases are of biomedical interest because of their roles in the regulation of gene expression and protein biosynthesis. Human JmjC 2OG oxygenases catalyze oxidative modifications to give either chemically stable alcohol products, o...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Elsevier
2016
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| _version_ | 1826284237554188288 |
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| author | Markolovic, S Leissing, T Chowdhury, R Wilkins, S Lu, X Schofield, C |
| author_facet | Markolovic, S Leissing, T Chowdhury, R Wilkins, S Lu, X Schofield, C |
| author_sort | Markolovic, S |
| collection | OXFORD |
| description | The Jumonji-C (JmjC) subfamily of 2-oxoglutarate (2OG)-dependent oxygenases are of biomedical interest because of their roles in the regulation of gene expression and protein biosynthesis. Human JmjC 2OG oxygenases catalyze oxidative modifications to give either chemically stable alcohol products, or in the case of N(ɛ)-methyl lysine demethylation, relatively unstable hemiaminals that fragment to give formaldehyde and the demethylated product. Recent work has yielded conflicting reports as to whether some JmjC oxygenases catalyze N-methyl group demethylation or hydroxylation reactions. We review JmjC oxygenase-catalyzed reactions within the context of structural knowledge, highlighting key differences between hydroxylases and demethylases, which have the potential to inform on the possible type(s) of reactions catalyzed by partially characterized or un-characterized JmjC oxygenases in humans and other organisms. |
| first_indexed | 2024-03-07T01:10:52Z |
| format | Journal article |
| id | oxford-uuid:8cf46d5d-9d37-4b2b-8e67-536f8ea5cd38 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:10:52Z |
| publishDate | 2016 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:8cf46d5d-9d37-4b2b-8e67-536f8ea5cd382022-03-26T22:48:03ZStructure–function relationships of human JmjC oxygenases — demethylases versus hydroxylasesJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8cf46d5d-9d37-4b2b-8e67-536f8ea5cd38EnglishSymplectic Elements at OxfordElsevier2016Markolovic, SLeissing, TChowdhury, RWilkins, SLu, XSchofield, CThe Jumonji-C (JmjC) subfamily of 2-oxoglutarate (2OG)-dependent oxygenases are of biomedical interest because of their roles in the regulation of gene expression and protein biosynthesis. Human JmjC 2OG oxygenases catalyze oxidative modifications to give either chemically stable alcohol products, or in the case of N(ɛ)-methyl lysine demethylation, relatively unstable hemiaminals that fragment to give formaldehyde and the demethylated product. Recent work has yielded conflicting reports as to whether some JmjC oxygenases catalyze N-methyl group demethylation or hydroxylation reactions. We review JmjC oxygenase-catalyzed reactions within the context of structural knowledge, highlighting key differences between hydroxylases and demethylases, which have the potential to inform on the possible type(s) of reactions catalyzed by partially characterized or un-characterized JmjC oxygenases in humans and other organisms. |
| spellingShingle | Markolovic, S Leissing, T Chowdhury, R Wilkins, S Lu, X Schofield, C Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases |
| title | Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases |
| title_full | Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases |
| title_fullStr | Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases |
| title_full_unstemmed | Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases |
| title_short | Structure–function relationships of human JmjC oxygenases — demethylases versus hydroxylases |
| title_sort | structure function relationships of human jmjc oxygenases demethylases versus hydroxylases |
| work_keys_str_mv | AT markolovics structurefunctionrelationshipsofhumanjmjcoxygenasesdemethylasesversushydroxylases AT leissingt structurefunctionrelationshipsofhumanjmjcoxygenasesdemethylasesversushydroxylases AT chowdhuryr structurefunctionrelationshipsofhumanjmjcoxygenasesdemethylasesversushydroxylases AT wilkinss structurefunctionrelationshipsofhumanjmjcoxygenasesdemethylasesversushydroxylases AT lux structurefunctionrelationshipsofhumanjmjcoxygenasesdemethylasesversushydroxylases AT schofieldc structurefunctionrelationshipsofhumanjmjcoxygenasesdemethylasesversushydroxylases |