| Function | Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. More than 95% of the BAs are N-acyl amidates with glycine and taurine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption. May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs. |
| Protein Name | Bile Acid-Coa -Amino Acid N-AcyltransferaseBacatBatBile Acid-Coa ThioesteraseCholoyl-Coa HydrolaseGlycine N-CholoyltransferaseLong-Chain Fatty-Acyl-Coa Hydrolase |
| Database Links | Reactome: R-HSA-159418Reactome: R-HSA-193368Reactome: R-HSA-9033241 |
| Cellular Localisation | CytoplasmCytosolPeroxisome |
| Alternative Protein Names | Bile Acid-Coa -Amino Acid N-Acyltransferase proteinBacat proteinBat proteinBile Acid-Coa Thioesterase proteinCholoyl-Coa Hydrolase proteinGlycine N-Choloyltransferase proteinLong-Chain Fatty-Acyl-Coa Hydrolase proteinBAAT protein |
Information sourced from Uniprot.org
