期刊
BIOLOGICAL CHEMISTRY
卷 400, 期 5, 页码 575-587出版社
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2018-0319
关键词
disulfide; Grx; PDI; pKa; thiol-disulfide exchange; Trx
资金
- European Union (FEDER) [POCI/01/0145/FEDER/007728]
- National Funds (Fundacao para a Ciencia e Tecnologia)
- (Ministerio da Educacao e Ciencia - FCT/MEC) [UID/MULTI/04378/2013, NORTE-01-0145-FEDER-000024]
- Norte Portugal Regional Operational Programme (NORTE 2020), under the PORTUGAL 2020 Partnership Agreement, through the European Regional Development Fund (ERDF)
- Fundacao para a Ciencia e a Tecnologia (FCT) [IF/00052/2014]
- Erasmus Mundus Programme of the European Master in Theoretical Chemistry and Computational Modelling (EMTCCM)
- European Union
Disulfide bonds play a critical role in a variety of structural and mechanistic processes associated with proteins inside the cells and in the extracellular environment. The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction. Here, we review the structural and mechanistic determinants behind the thiol-disulfide exchange reactions for the different enzyme types within this family, rationalizing the known experimental data in light of the results from computational studies. The analysis sheds new atomic-level insight into the structural and mechanistic variations that characterize the different enzymes in the family, helping to explain the associated functional diversity. Furthermore, we review here a pattern of stabilization/destabilization of the conserved active-site cysteine residues presented beforehand, which is fully consistent with the observed roles played by the thioredoxin family of enzymes.
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