[HTML][HTML] Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues
SI Hashemy, A Holmgren - Journal of Biological Chemistry, 2008 - ASBMB
The mammalian cytosolic/nuclear thioredoxin system, comprising thioredoxin (Trx),
selenoenzyme thioredoxin reductase (TrxR), and NADPH, is the major protein-disulfide
reductase of the cell and has numerous functions. The active site of reduced Trx comprises
Cys 32-Gly-Pro-Cys 35 thiols that catalyze target disulfide reduction, generating a disulfide.
Human Trx1 has also three structural Cys residues in positions 62, 69, and 73 that upon
diamide oxidation induce a second Cys 62–Cys 69 disulfide as well as dimers and …
selenoenzyme thioredoxin reductase (TrxR), and NADPH, is the major protein-disulfide
reductase of the cell and has numerous functions. The active site of reduced Trx comprises
Cys 32-Gly-Pro-Cys 35 thiols that catalyze target disulfide reduction, generating a disulfide.
Human Trx1 has also three structural Cys residues in positions 62, 69, and 73 that upon
diamide oxidation induce a second Cys 62–Cys 69 disulfide as well as dimers and …