Enzymatic Phosphorylation of Oxidized Tyrosine Residues.
insulin receptor
liquid chromatography-tandem mass spectrometry (LC-MS/MS)
mass spectrometry (MS)
oxidation−reduction (redox)
phosphorylation
post-translational modification (PTM)
ultra-high-performance liquid chromatography (UHPLC)
Journal
Journal of proteome research
ISSN: 1535-3907
Titre abrégé: J Proteome Res
Pays: United States
ID NLM: 101128775
Informations de publication
Date de publication:
02 06 2023
02 06 2023
Historique:
medline:
5
6
2023
pubmed:
5
5
2023
entrez:
5
5
2023
Statut:
ppublish
Résumé
Post-translational modifications (PTMs) alter the function and fate of proteins and cells in almost every conceivable way. Protein modifications can occur as a result of specific regulating actions of enzymes, such as tyrosine kinases phosphorylating tyrosine residues or by nonenzymatic reactions, such as oxidation related to oxidative stress and diseases. While many studies have addressed the multisite, dynamic, and network-like properties of PTMs, only little is known of the interplay of the same site modifications. In this work, we studied the enzymatic phosphorylation of oxidized tyrosine (l-DOPA) residues using synthetic insulin receptor peptides, in which tyrosine residues were replaced with l-DOPA. The phosphorylated peptides were identified by liquid chromatography-high-resolution mass spectrometry and the site of phosphorylation by tandem mass spectrometry. The results clearly show that the oxidized tyrosine residues are phosphorylated, displaying a specific immonium ion peak in the MS
Identifiants
pubmed: 37146082
doi: 10.1021/acs.jproteome.3c00061
pmc: PMC10243104
doi:
Substances chimiques
Tyrosine
42HK56048U
Levodopa
46627O600J
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1959-1968Références
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