Glutaric acid is made from lysine & tryptophan via alphaketo-adipic acid.

- Elevated in the genetic diseases glutaric academia types I and II.
- Moderate increases may be due to deficiencies in riboflavin and coenzyme Q10, or celiac disease.
- Moderate increases are common in autism possibly due to defective vitamin absorption or microbial production in the GI tract.

Glutaric acid is made from lysine & tryptophan via alphaketo-adipic acid.

- Elevated in the genetic diseases glutaric academia types I and II.
- Moderate increases may be due to deficiencies in riboflavin and coenzyme Q10, or celiac disease.
- Moderate increases are common in autism possibly due to defective vitamin absorption or microbial production in the GI tract.

Glutaric acid is made from lysine & tryptophan via alphaketo-adipic acid.

- Elevated in the genetic diseases glutaric academia types I and II.
- Moderate increases may be due to deficiencies in riboflavin and coenzyme Q10, or celiac disease.
- Moderate increases are common in autism possibly due to defective vitamin absorption or microbial production in the GI tract.

Glutaric Acid (Glutarate) is endogenously produced in the catabolism of lysine and tryptophan.

- Increased Glutaric acid is associated with secondary carnitine deficiency.

- Glutaryl-CoA (from lysine or tryptophan) normally enters the Krebs cycle via transition to acetyl-CoA.

    » Glutaryl-CoA dehydrogenase (GCDH) + glutaryl-CoA + B2 → acetyl-CoA.

    » If GCDH is blocked, glutaryl-CoA + carnitine → elevated glutaric acid.

Glutaric Acid is formed from the essential amino acids lysine and tryptophan through the intermediaries of alpha ketoadipic acid and glutaryl-CoA. Glutaryl-CoA is further metabolized to glutaconyl- and crotonyl-CoA by an enzyme called glutaryl-CoA dehydrogenase. This enzyme requires riboflavin (vitamin B2) as a cofactor.

Glutaric acid is a breakdown product of lysine and/or tryptophan.

Glutaric Acid is formed from the essential amino acids lysine and tryptophan through the intermediaries of alpha ketoadipic acid and glutaryl-CoA. Glutaryl-CoA is further metabolized to glutaconyl- and crotonyl-CoA by an enzyme called glutaryl-CoA dehydrogenase. This enzyme requires riboflavin (vitamin B2) as a cofactor.

Glutaric Acid is formed from the essential amino acids lysine and tryptophan through the intermediaries of alpha ketoadipic acid and glutaryl-CoA. Glutaryl-CoA is further metabolized to glutaconyl- and crotonyl-CoA by an enzyme called glutaryl-CoA dehydrogenase. This enzyme requires riboflavin (vitamin B2) as a cofactor.

Glutathione (GSH) is a tripeptide comprised of three amino acids (cysteine, glycine, and glutamic acid). Glutathione is the body’s most potent intracellular antioxidant. It exists intracellularly in either an oxidized or reduced state.

GSH acts as an antioxidant, free radical scavenger, and detoxifying agent. Excessive formation of reactive oxygen species (ROS), including hydrogen peroxide (H2O2), is toxic to the cell. Hence, the metabolism of these free radicals are critical, and they are tightly controlled. [L]

Glutathione is implicated in many cellular functions including antioxidant protection and detoxification. It is also essential for the maintenance of cell membrane integrity in red blood cells.

Glutathione (oxidized) measures GSSG—the form of glutathione created after neutralizing oxidative stress. Elevated levels may indicate increased oxidative burden, inflammation, or reduced ability to recycle glutathione back into its active form (GSH). This test helps assess antioxidant capacity and overall redox balance.

Glutathione (reduced), or GSH, is the body’s primary intracellular antioxidant and detoxification molecule. This marker reflects the availability of active glutathione needed to neutralize free radicals, support liver detoxification, and maintain redox balance. Low GSH suggests increased oxidative stress, nutrient deficiencies, or impaired glutathione synthesis or recycling.

Glutathione (GSH) is composed of cysteine, glutamine & glycine. GSH is a source of sulfate and plays a key role in antioxidant activity and detoxification of toxins.

Glutathione is the most powerful antioxidant in the human body. It is found in nearly every cell in the body and is the primary agent of detoxification in the liver. Glutathione can also act as a hormone, regulating the release of GABA and dopamine. Glutathione is produced from three amino acids glutamate, cysteine, and glycine which are obtained from food or supplementation. Deficiency in glutathione may lead to production of free radicals and oxidative damage throughout the body. Recent evidence suggests that the gut microbiome determines levels of glutathione throughout the body.

Glutathione (GSH) is a tripeptide (λ-glutamyl-cysteinylglycine) synthesized by most cells, serving as a critical marker of cellular health and resilience against toxic stress. In erythrocytes, GSH levels are a sensitive indicator of the body's intracellular GSH status and overall cellular well-being. It is the most abundant non-protein thiol in mammalian cells, playing key roles in various biological processes, such as detoxifying harmful compounds (xenobiotics), neutralizing reactive oxygen species, regulating cellular redox balance, and maintaining the oxidative state of vital protein sulfhydryl groups. Additionally, GSH supports immune function. Intracellular GSH concentrations are significantly higher than plasma levels, with plasma GSH largely derived from the liver.