Journal article
A human protein hydroxylase that accepts D-residues
- Abstract:
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Factor inhibiting hypoxia-inducible factor (FIH) is a 2-oxoglutarate-dependent protein hydroxylase that catalyses C3 hydroxylations of protein residues. We report FIH can accept (D)- and (L)-residues for hydroxylation. The substrate selectivity of FIH differs for (D) and (L) epimers, e.g., (D)- but not (L)-allylglycine, and conversely (L)- but not (D)-aspartate, undergo monohydroxylation, in the tested sequence context. The (L)-Leu-containing substrate undergoes FIH-catalysed monohydroxylatio...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, 2.2MB)
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(Version of record, 1.5MB)
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- Publisher copy:
- 10.1038/s42004-020-0290-5
Authors
Bibliographic Details
- Publisher:
- Springer Nature Publisher's website
- Journal:
- Communications Chemistry Journal website
- Volume:
- 3
- Article number:
- 52
- Publication date:
- 2020-05-01
- Acceptance date:
- 2020-03-12
- DOI:
- EISSN:
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2399-3669
Item Description
- Language:
- English
- Keywords:
- Subjects:
- Pubs id:
-
1102494
- Local pid:
- pubs:1102494
- Deposit date:
- 2020-04-30
Terms of use
- Copyright holder:
- Choi, H et al.
- Copyright date:
- 2020
- Rights statement:
- © The Author(s) 2020. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
- Licence:
- CC Attribution (CC BY)
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