Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.
Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment pr...
| Main Authors: | , , , , , |
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| 格式: | Journal article |
| 语言: | English |
| 出版: |
2002
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| _version_ | 1826290897597235200 |
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| author | McNeill, L Hewitson, K Claridge, T Seibel, J Horsfall, L Schofield, C |
| author_facet | McNeill, L Hewitson, K Claridge, T Seibel, J Horsfall, L Schofield, C |
| author_sort | McNeill, L |
| collection | OXFORD |
| description | Asparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo -isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro -isomer. |
| first_indexed | 2024-03-07T02:51:13Z |
| format | Journal article |
| id | oxford-uuid:adbef5f2-e95e-4b67-bfcb-fe9077a00bd3 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:51:13Z |
| publishDate | 2002 |
| record_format | dspace |
| spelling | oxford-uuid:adbef5f2-e95e-4b67-bfcb-fe9077a00bd32022-03-27T03:37:51ZHypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:adbef5f2-e95e-4b67-bfcb-fe9077a00bd3EnglishSymplectic Elements at Oxford2002McNeill, LHewitson, KClaridge, TSeibel, JHorsfall, LSchofield, CAsparagine-803 in the C-terminal transactivation domain of human hypoxia-inducible factor (HIF)-1 alpha-subunit is hydroxylated by factor inhibiting HIF-1 (FIH-1) under normoxic conditions causing abrogation of the HIF-1alpha/p300 interaction. NMR and other analyses of a hydroxylated HIF fragment produced in vitro demonstrate that hydroxylation occurs at the beta-carbon of Asn-803 and imply production of the threo -isomer, in contrast with other known aspartic acid/asparagine hydroxylases that produce the erythro -isomer. |
| spellingShingle | McNeill, L Hewitson, K Claridge, T Seibel, J Horsfall, L Schofield, C Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. |
| title | Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. |
| title_full | Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. |
| title_fullStr | Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. |
| title_full_unstemmed | Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. |
| title_short | Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803. |
| title_sort | hypoxia inducible factor asparaginyl hydroxylase fih 1 catalyses hydroxylation at the beta carbon of asparagine 803 |
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