Thioredoxin
From Proteopedia
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Alexander Berchansky, Laura Maria Batista Leal, Joel L. Sussman, Michal Harel
FunctionThioredoxin (Trx) is an enzyme which facilitates, in its reduced form, the reduction of proteins by cysteine thiol-disulfide exchange[1]. They contain a CXXC motif.
There are a range of strategies used by the host organism in an attempt to defend itself against pathogen invasion. Among these is the release of oxidants, such as reactive oxygen species (ROS), which at defined physiological concentrations act as signaling messengers. However, in supraphysiological concentrations, their reactivity has deleterious cellular consequences, causing damage to macromolecules such as proteins, lipids and DNA, thus impairing the system's homeostasis (SIES, 1985). It is therefore an alternative used to inhibit the pathogen and prevent infection of the organism.
RelevanceSerum Trx level is a predictor of steatohepatitis[2]. DiseaseTrx is involved in a wide range of human diseases and conditions including cancer, viral diseases, aging, cardiac conditions and more[3]. Structural highlightsThe active site motif Cys-Gly-Pro-Cys is involved in the reduction of disulfide bonds in proteins[4] 3D Structures of Thioredoxin
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Alexander Berchansky, Laura Maria Batista Leal, Joel L. Sussman, Michal Harel
This page was last modified 11:57, 23 June 2025.