TXNL1 has dual functions as a redox active thioredoxin-like protein as well as an ATP- and redox-independent chaperone.
Chaperone
Disulfide
Insulin
Reduction
Thioredoxin
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
11 2023
11 2023
Historique:
received:
11
08
2023
revised:
17
09
2023
accepted:
18
09
2023
medline:
30
10
2023
pubmed:
8
10
2023
entrez:
7
10
2023
Statut:
ppublish
Résumé
TXNL1 (also named TRP32, for thioredoxin related protein of 32 kDa) is a cytosolic thioredoxin-fold protein expressed in all cell types and conserved from yeast to mammals, but with yet poorly known function. Here, we expressed and purified human TXNL1 together with several Cys-to-Ser variants, characterizing their enzymatic properties. TXNL1 could reduce disulfides in insulin, cystine and glutathione disulfide (GSSG) in reactions coupled to thioredoxin reductase (TXNRD1, TrxR1) using NADPH, similarly to thioredoxin (TXN, Trx1), but with lower catalytic efficacy due to at least one order of magnitude higher K
Identifiants
pubmed: 37804695
pii: S2213-2317(23)00298-7
doi: 10.1016/j.redox.2023.102897
pmc: PMC10570131
pii:
doi:
Substances chimiques
NADP
53-59-8
Cystine
48TCX9A1VT
Thioredoxins
52500-60-4
Thioredoxin-Disulfide Reductase
EC 1.8.1.9
Insulins
0
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102897Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.