The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues.
Amino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfami...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
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2011
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| _version_ | 1826258197973827584 |
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| author | Mantri, M Loik, N Hamed, R Claridge, T McCullagh, J Schofield, C |
| author_facet | Mantri, M Loik, N Hamed, R Claridge, T McCullagh, J Schofield, C |
| author_sort | Mantri, M |
| collection | OXFORD |
| description | Amino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfamily of lysyl hydroxylases has evolved and illustrates the importance of stereochemical assignments in proteomic analyses. |
| first_indexed | 2024-03-06T18:30:12Z |
| format | Journal article |
| id | oxford-uuid:095b4ccb-bdaa-4648-95c0-34a596706a4f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:30:12Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:095b4ccb-bdaa-4648-95c0-34a596706a4f2022-03-26T09:18:04ZThe 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:095b4ccb-bdaa-4648-95c0-34a596706a4fEnglishSymplectic Elements at Oxford2011Mantri, MLoik, NHamed, RClaridge, TMcCullagh, JSchofield, CAmino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfamily of lysyl hydroxylases has evolved and illustrates the importance of stereochemical assignments in proteomic analyses. |
| spellingShingle | Mantri, M Loik, N Hamed, R Claridge, T McCullagh, J Schofield, C The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. |
| title | The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. |
| title_full | The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. |
| title_fullStr | The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. |
| title_full_unstemmed | The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. |
| title_short | The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. |
| title_sort | 2 oxoglutarate dependent oxygenase jmjd6 catalyses oxidation of lysine residues to give 5s hydroxylysine residues |
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