Bile acid-CoA:amino acid N-acyltransferase

Definition

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.

References:

[1]. M R Johnson, et al. Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J Biol Chem. 1991 Jun 5;266(16):10227-33. [Content Brief]

[2]. James O'Byrne, et al. The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J Biol Chem. 2003 Sep 5;278(36):34237-44. [Content Brief]

[3]. Mindan K Sfakianos, et al. Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. J Biol Chem. 2002 Dec 6;277(49):47270-5. [Content Brief]

[4]. C N Falany, et al. Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [Content Brief]

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