Bile acid-CoA:amino acid N-acyltransferase (BAAT) (BAAT)

Bile acid-CoA:amino acid N-acyltransferase (BAAT) is a liver-specific enzyme that plays a pivotal role in the terminal step of bile acid synthesis by conjugating bile acids with glycine or taurine (UniProt P35269). This conjugation process is essential for increasing the solubility and amphipathic properties of bile acids, enabling them to form micelles that facilitate the digestion and absorption of dietary fats and fat-soluble vitamins in the small intestine (PubMed: 15190246). BAAT is primarily localized in the peroxisomes and cytosol of hepatocytes. Genetic deficiencies in the BAAT gene are associated with familial hypercholanemia, a condition characterized by elevated serum unconjugated bile acids, fat malabsorption, and fat-soluble vitamin deficiencies (OMIM: 602938). While there are currently no FDA-approved drugs that specifically target BAAT, it is an area of active research for treating metabolic disorders, as modulating the bile acid pool can influence systemic glucose and lipid metabolism (PubMed: 25611108). Experimental inhibitors have been studied in animal models to explore their potential in managing obesity and metabolic syndrome.

Other names

Bile acid-CoA:glycine/taurine N-acyltransferaseGlycine N-choloyltransferaseTaurine N-choloyltransferaseBATBACATLong-chain fatty-acyl-CoA hydrolase

BAAT catalyzes the conjugation of primary and secondary bile acids with the amino acids glycine or taurine, a critical step for the formation of amphipathic bile salts (UniProt P35269).