Enzymes > Bile acid-CoA:amino acid N-acyltransferase (BAAT)
Bile acid-CoA:amino acid N-acyltransferase (BAAT)
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UniProt Number:
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Q14032
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Alternate Names:
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glycine N-choloyltransferase, long-chain fatty-acyl-CoA hydrolase, BACAT, BAT
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Structure and Function:
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BAAT is a cytoplasmic monomeric enzyme found in liver tissue, gallbladder mucosa and pancreas. BAAT is involved in bile acid metabolism. In liver hepatocytes, BAAT catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. This enzyme may also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro BAAT 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. In humans, more than 95% of the biliary bile acids are N-acyl amidates with glycine and taurine. In other mammalian species, large differences are observed in the relative amounts of taurine- and glycine-conjugated bile acids formed in bile.
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Disease Associations:
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Defects in BAAT are involved in familial hypercholanemia (FHCA) [MIM:607748]. FHCA is a disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.
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Protein Quantity Assays
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CART
