Glutathione S-transferase

Glutathione S-transferase (pronunciation: glu·ta·thi·one S-trans·fer·ase, abbreviated as GST) is a family of enzymes that play a crucial role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione.

Etymology

The term "Glutathione S-transferase" is derived from the name of the glutathione molecule, a tripeptide consisting of three amino acids: glutamate, cysteine, and glycine. The "S" in the name refers to the sulfur atom of the cysteine in the glutathione molecule, which is the site of the transferase reaction. The term "transferase" refers to the class of enzymes that catalyze the transfer of a functional group from one molecule to another.

Function

Glutathione S-transferases are involved in the detoxification of a wide variety of xenobiotic and endobiotic compounds. They catalyze the conjugation of the reduced form of glutathione to xenobiotic substrates for the purpose of making the compounds more water-soluble. This process is critical for the body's defense against harmful compounds, as it allows for their excretion from the body.

Related Terms

Enzyme: A protein that acts as a biological catalyst to speed up a chemical reaction.
Detoxification: The process of removing toxic substances from the body.
Glutathione: A tripeptide consisting of three amino acids: glutamate, cysteine, and glycine.
Amino Acids: Organic compounds that combine to form proteins.
Xenobiotic: A foreign compound or substance not naturally produced by the body.
Endobiotic: A compound or substance naturally produced by the body.