ADY tripeptide is a minimum sequence for Tyrosylprotein sulfotransferases 1 and 2 substrate recognition.
Synthetic peptide
Tyrosine sulfation
Tyrosylprotein sulfotransferases
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
08 10 2023
08 10 2023
Historique:
received:
07
07
2023
accepted:
13
07
2023
medline:
4
9
2023
pubmed:
26
7
2023
entrez:
25
7
2023
Statut:
ppublish
Résumé
Tyrosylprotein sulfotransferases (TPSTs) catalyze the transfer of a sulphonate moiety from 3'-Phosphoadenosine 5'-Phosphosulfate (PAPS) to the hydroxyl group of a tyrosine residue in substrate proteins. The positively charged substrate binding region of TPST homodimer interacts with acidic residues located in N-terminal region from the sulfated tyrosine in substrates. However, the sequence pattern in TPST substrate recognition remains unclear. Therefore, we aimed to determine the minimum recognition chain length required for tyrosine sulfation. We prepared His-tagged polypeptide, His-TPST1
Identifiants
pubmed: 37490834
pii: S0006-291X(23)00883-5
doi: 10.1016/j.bbrc.2023.07.026
pii:
doi:
Substances chimiques
Peptides
0
Sulfates
0
Tyrosine
42HK56048U
Sulfotransferases
EC 2.8.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
73-77Informations de copyright
Copyright © 2023 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Shinichi Asada reports equipment, drugs, or supplies was provided by Japan Society for the Promotion of Science.