Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor.
Substrate specificity: Biochemical and crystallographic analyses reveal the hypoxia-inducible factor hydroxylase (FIH) as being promiscuous with respect to the residues that it can hydroxylate in β-position, which in addition to Asn, Asp, and His include Leu and Ser residues. The Ser substrate is ox...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2013
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| _version_ | 1797089986307162112 |
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| author | Yang, M Hardy, A Chowdhury, R Loik, N Scotti, J McCullagh, J Claridge, T McDonough, M Ge, W Schofield, C |
| author_facet | Yang, M Hardy, A Chowdhury, R Loik, N Scotti, J McCullagh, J Claridge, T McDonough, M Ge, W Schofield, C |
| author_sort | Yang, M |
| collection | OXFORD |
| description | Substrate specificity: Biochemical and crystallographic analyses reveal the hypoxia-inducible factor hydroxylase (FIH) as being promiscuous with respect to the residues that it can hydroxylate in β-position, which in addition to Asn, Asp, and His include Leu and Ser residues. The Ser substrate is oxidized to an epimeric β-geminal diol product (see picture). Copyright © 2013 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim. |
| first_indexed | 2024-03-07T03:11:57Z |
| format | Journal article |
| id | oxford-uuid:b47f0d6c-c29a-4ac5-a4cb-c3ba5d306c3d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:11:57Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | oxford-uuid:b47f0d6c-c29a-4ac5-a4cb-c3ba5d306c3d2022-03-27T04:26:32ZSubstrate selectivity analyses of factor inhibiting hypoxia-inducible factor.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b47f0d6c-c29a-4ac5-a4cb-c3ba5d306c3dEnglishSymplectic Elements at Oxford2013Yang, MHardy, AChowdhury, RLoik, NScotti, JMcCullagh, JClaridge, TMcDonough, MGe, WSchofield, CSubstrate specificity: Biochemical and crystallographic analyses reveal the hypoxia-inducible factor hydroxylase (FIH) as being promiscuous with respect to the residues that it can hydroxylate in β-position, which in addition to Asn, Asp, and His include Leu and Ser residues. The Ser substrate is oxidized to an epimeric β-geminal diol product (see picture). Copyright © 2013 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim. |
| spellingShingle | Yang, M Hardy, A Chowdhury, R Loik, N Scotti, J McCullagh, J Claridge, T McDonough, M Ge, W Schofield, C Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. |
| title | Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. |
| title_full | Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. |
| title_fullStr | Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. |
| title_full_unstemmed | Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. |
| title_short | Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. |
| title_sort | substrate selectivity analyses of factor inhibiting hypoxia inducible factor |
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