Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins

• Tipo: Outra Publicação em Revista Científica Internacional
• Data: 2019

Autores

Sergio Filipe Sousa (Autor) FCUP; Neves, RPP (Autor) FCUP; Waheed, SO (Autor) Outra; Pedro A Fernandes (Autor) FCUP; Ramos, MJ (Autor) FCUP

Revista

A Revista está pendente de validação pelos Serviços Administrativos.

Título: BIOLOGICAL CHEMISTRY

Vol. 400

Páginas: 575-587

ISSN: 1431-6730

Editora: Walter de Gruyter GmbH

Indexação

ISI Web of Knowledge - 14 Citações

Scopus - 16 Citações

Outras Informações

ID Authenticus: P-00P-VKW

DOI: 10.1515/hsz-2018-0319

Abstract (EN): 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 13