Kinetic and inhibition studies on human Jumonji-C (JmjC) domain-containing protein 5.
Journal
RSC chemical biology
ISSN: 2633-0679
Titre abrégé: RSC Chem Biol
Pays: England
ID NLM: 101768727
Informations de publication
Date de publication:
07 Jun 2023
07 Jun 2023
Historique:
received:
16
12
2022
accepted:
19
03
2023
medline:
9
6
2023
pubmed:
9
6
2023
entrez:
9
6
2023
Statut:
epublish
Résumé
Jumonji-C (JmjC) domain-containing protein 5 (JMJD5) is a human 2-oxoglutarate (2OG) and Fe(ii)-dependent oxygenase which catalyses the post-translational C3 hydroxylation of arginyl-residues and which is linked to the circadian rhythm and to cancer biology through as yet unidentified mechanisms. We report robust solid phase extraction coupled to mass spectrometry (SPE-MS)-based JMJD5 assays which enable kinetic and high-throughput inhibition studies. The kinetic studies reveal that some synthetic 2OG derivatives, notably including a 2OG derivative with a cyclic carbon backbone (
Identifiants
pubmed: 37292060
doi: 10.1039/d2cb00249c
pii: d2cb00249c
pmc: PMC10246557
doi:
Types de publication
Journal Article
Langues
eng
Pagination
399-413Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
There are no conflicts to declare.
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