Mechanistic insights into the urea-induced denaturation of a non-seleno thiol specific antioxidant human peroxiredoxin 6.
Antioxidants
/ chemistry
Humans
Hydrogen Bonding
Molecular Dynamics Simulation
Peroxiredoxin VI
/ chemistry
Protein Conformation
Protein Denaturation
/ drug effects
Protein Unfolding
Solvents
Spectrum Analysis
Structure-Activity Relationship
Sulfhydryl Compounds
/ chemistry
Thermodynamics
Urea
/ chemistry
Molecular dynamics simulation
Peroxiredoxin
Protein folding and stability
Urea-induced chemical denaturation
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
15 Oct 2020
15 Oct 2020
Historique:
received:
05
04
2020
revised:
18
05
2020
accepted:
19
05
2020
pubmed:
3
6
2020
medline:
30
3
2021
entrez:
3
6
2020
Statut:
ppublish
Résumé
Peroxiredoxin 6 (Prdx6) is a unique enzyme among mammalian peroxiredoxins as it lacks resolving cysteine. It is found to be involved in number of different diseases including tumours and its expression level is highest in lungs as compared to other organs. It has been found that Prdx6 plays a significant role different metabolic diseases, ocular damage, neurodegeneration and male infertility. It is a bifunctional protein having phospholipase A
Identifiants
pubmed: 32485253
pii: S0141-8130(20)33315-8
doi: 10.1016/j.ijbiomac.2020.05.168
pii:
doi:
Substances chimiques
Antioxidants
0
Solvents
0
Sulfhydryl Compounds
0
Urea
8W8T17847W
Peroxiredoxin VI
EC 1.11.1.15
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1171-1180Informations de copyright
Copyright © 2018 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest Authors declare there is no conflict of interest.