Taurine—2-oxoglutarate transaminase

From WikiMD's Wellness Encyclopedia

Taurine—2-oxoglutarate transaminase (also known as tauD or TDO) is an enzyme that catalyzes the chemical reaction between Taurine and 2-oxoglutarate to produce L-glutamate and sulfoacetaldehyde. This enzyme plays a crucial role in the metabolism of taurine, an important amino acid in many biological systems, including humans. Taurine—2-oxoglutarate transaminase is involved in the Cysteine and methionine metabolism pathway, highlighting its importance in sulfur amino acid metabolism.

Function[edit | edit source]

Taurine—2-oxoglutarate transaminase is essential for the degradation of taurine, a compound that participates in a variety of physiological processes such as bile acid conjugation, osmoregulation, and modulation of calcium signaling. By converting taurine into sulfoacetaldehyde, this enzyme facilitates the removal of excess taurine from the body and participates in the recycling of sulfur-containing amino acids.

Structure[edit | edit source]

The enzyme belongs to the family of transaminases, which all share a common mechanism involving the transfer of an amino group from an amino acid to an alpha-keto acid. The active site of taurine—2-oxoglutarate transaminase typically contains a pyridoxal phosphate (PLP) cofactor, which is essential for its catalytic activity.

Clinical Significance[edit | edit source]

Alterations in the activity of taurine—2-oxoglutarate transaminase can have significant implications for human health. Given its role in taurine metabolism, abnormalities in this enzyme's function can lead to disturbances in taurine levels, which have been associated with various conditions such as cardiovascular diseases, neurological disorders, and metabolic syndrome. Research into the regulation and function of this enzyme may provide insights into novel therapeutic strategies for these conditions.

Genetic Regulation[edit | edit source]

The gene encoding taurine—2-oxoglutarate transaminase is regulated by various factors, including nutritional status and hormonal signals. Understanding the genetic regulation of this enzyme is crucial for elucidating the complex network of interactions that govern amino acid metabolism and homeostasis in the body.

See Also[edit | edit source]

References[edit | edit source]


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Contributors: Prab R. Tumpati, MD