A human protein hydroxylase that accepts D-residues.
Journal
Communications chemistry
ISSN: 2399-3669
Titre abrégé: Commun Chem
Pays: England
ID NLM: 101725670
Informations de publication
Date de publication:
01 May 2020
01 May 2020
Historique:
received:
14
10
2019
accepted:
12
03
2020
entrez:
27
1
2023
pubmed:
1
5
2020
medline:
1
5
2020
Statut:
epublish
Résumé
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 monohydroxylation, whereas (D)-Leu unexpectedly undergoes dihydroxylation. Crystallographic, mass spectrometric, and DFT studies provide insights into the selectivity of FIH towards (L)- and (D)-residues. The results of this work expand the potential range of known substrates hydroxylated by isolated FIH and imply that it will be possible to generate FIH variants with altered selectivities.
Identifiants
pubmed: 36703414
doi: 10.1038/s42004-020-0290-5
pii: 10.1038/s42004-020-0290-5
pmc: PMC9814778
doi:
Types de publication
Journal Article
Langues
eng
Pagination
52Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L009846/1
Pays : United Kingdom
Organisme : Cancer Research UK (CRUK)
ID : C9047/A24759
Organisme : Wellcome Trust (Wellcome)
ID : 091857/7/10/7
Informations de copyright
© 2020. The Author(s).
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