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. 2020 May 1;3:52. doi: 10.1038/s42004-020-0290-5

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© 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. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — FIH is a 2OG oxygenase catalyzing the posttranslational C3 hydroxylation of (L)-residue substrates including the hypoxia-inducible factor α-subunits (HIFα; R = CONH₂) and ankyrin repeat domain proteins (R = CONH₂, COOH, OH, imidazole and isopropyl) to give mono-hydroxylated products. Note all studied (L)/(2S)-substrates give products with the same relative stereochemistry at C3, i.e., (2S,3S) for R = CONH₂, COOH, Imidazole, OH or (2S,3R) for R = ⁱPr.