background:
The UDP-Glucuronosyltransferases (UGT) comprise a family of enzymes that detoxify and enhance the urinary excretion of a wide variety of xenobiotic and endogenous substrates by transferring glucuronic acid to sulfhydryl, hydroxyl, aromatic amino, or carboxylic acid groups. They have been subdivided into two families, UGT1 and UGT2, based on the evolutionary divergence of their genes. The enzymes of the UGT1A family play an important role in the metabolism of dietary constituents, phenols, and therapeutic drugs, and also the glucuronidation of bilirubin and iodothyronines. The enzymes of the UGT2B family are involved in the metabolism of bile acids, phenol derivatives, catecholestrogens and steroids. Although it is widely recognized that the liver is the major site of glucuronidation, it is now clear that UGT enzymes are also found in extra-hepatic tissues.
Function:
UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme is active on polyhydroxylated estrogens (such as estriol, 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (such as 4-methylumbelliferone, 1-naphthol, 4-nitrophenol, 2-aminophenol, 4-hydroxybiphenyl and menthol). It is capable of 6 alpha-hydroxyglucuronidation of hyodeoxycholic acid.
Subcellular Location:
Microsome membrane; Single-pass membrane protein (Potential). Endoplasmic reticulum membrane; Single-pass membrane protein (Potential).
Similarity:
Belongs to the UDP-glycosyltransferase family.
Database links:
UniProtKB/Swiss-Prot: P06133.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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