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2-Oxoglutarate derivatives can selectively enhance or inhibit the activity of human oxygenases

Abstract:
2-Oxoglutarate (2OG) oxygenases are validated agrochemical and human drug targets. The potential for modulating their activity with 2OG derivatives has not been explored, possibly due to concerns regarding selectivity. We report proof-of-principle studies demonstrating selective enhancement or inhibition of 2OG oxygenase activity by 2-oxo acids. The human 2OG oxygenases studied, factor inhibiting hypoxia-inducible transcription factor HIF-α (FIH) and aspartate/asparagine-β-hydroxylase (AspH), catalyze C3 hydroxylations of Asp/Asn-residues. Of 35 tested 2OG derivatives, 10 enhance and 17 inhibit FIH activity. Comparison with results for AspH reveals that 2OG derivatives selectively enhance or inhibit FIH or AspH. Comparison of FIH structures complexed with 2OG derivatives to those for AspH provides insight into the basis of the observed selectivity. 2-Oxo acid derivatives have potential as drugs, for use in biomimetic catalysis, and in functional studies. The results suggest that the in vivo activity of 2OG oxygenases may be regulated by natural 2-oxo acids other than 2OG.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-021-26673-2

Authors

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0002-0290-6565


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
12
Article number:
6478
Publication date:
2021-11-10
Acceptance date:
2021-10-12
DOI:
EISSN:
2041-1723


Language:
English
Keywords:
Pubs id:
1200953
Local pid:
pubs:1200953
Deposit date:
2021-10-12
ARK identifier:

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