Abstract:
: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.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Sousa SF,Neves RPP,Waheed SO,Fernandes PA,Ramos MJdoi
10.1515/hsz-2018-0319subject
Has Abstractpub_date
2019-04-24 00:00:00pages
575-587issue
5eissn
1431-6730issn
1437-4315pii
/j/bchm.just-accepted/hsz-2018-0319/hsz-2018-0319.journal_volume
400pub_type
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