Selenium proteins
Selenocysteine-containing enzymes
Also searched as Selenocysteine-containing enzymes.
Selenium has NO General Antioxidant Action of its own — it works only by being built into these specific enzymes, and there is a hierarchy: when supply is short, some selenoproteins are maintained and others are sacrificed. That hierarchy is why selenium status affects thyroid conversion and glutathione peroxidase differently.
In depth
The selenocysteine-containing enzymes — glutathione peroxidases, thioredoxin reductases and the deiodinases.
What drives it
Micronutrient status increases it.
Selenium is incorporated as selenocysteine. Carried by the intermediary-metabolism, micronutrient and clinical reviews. doi 10.3390/nu18132141 · PMC9967593
What it drives
It increases Master antioxidant.
Selenium has NO general antioxidant action of its own - it works only by being built into these enzymes. Glutathione peroxidase is a selenoprotein. Carried by the intermediary-metabolism, micronutrient and clinical reviews. doi 10.3390/nu18132141 · PMC9967593
It increases Thyroid.
The deiodinases are selenoproteins - which is why selenium status affects T4-to-T3 conversion. Carried by the intermediary-metabolism, micronutrient and clinical reviews. doi 10.3390/nu18132141 · PMC9967593
It reduces Oxidative stress.
Via glutathione peroxidase and thioredoxin reductase. Carried by the intermediary-metabolism, micronutrient and clinical reviews. doi 10.3390/nu18132141 · PMC9967593
It increases Thiol antioxidant system.
Thioredoxin reductase is a selenoprotein - selenium governs both reducing systems. Carried by the intermediary-metabolism, micronutrient and redox reviews. doi 10.3390/nu18132141 · PMC9967593
Blends that modulate it
Each blend page names this pathway and carries the study behind its claim.
See it on the map
Open the causal map to follow this pathway upstream and downstream, arrow by arrow, each with its study.