bile acid CoA:amino acid N-acyltransferase (BAT, BACAT, glycine N-choloyltransferase, long-chain fatty-acyl-CoA hydrolase, BAAT)
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Function
- bile acid metabolism
- in hepatocytes, catalyzes 2nd step in the conjugation of C24 bile acids (choloneates) to glycine & taurine before excretion into bile canaliculi
- may catalyze conjugation of primary or secondary bile acids, or both
- may also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids
- in vitro, catalyzes the hydrolysis of long- & very long-chain saturated acyl-CoAs to free fatty acid & coenzyme A & conjugates glycine to these acyl-CoAs
Choloyl-CoA + glycine <--> CoA + glycocholate
Palmitoyl-CoA + H2O <--> CoA + palmitate
- KM=1.1 mM for taurine toward choloyl-CoA;
- KM=2.2 mM for 2-fluoro-beta-alanine toward choloyl-CoA;
- KM=5.8 mM for glycine toward choloyl-CoA;
- KM=19.3 uM for arachidoyl-CoA;
- Vmax=0.33 umol/min/mg enzyme with taurine as substrate for acyltransferase activity;
- Vmax=0.19 umol/min/mg enzyme with 2-fluoro-beta-alanine as substrate for acyltransferase activity
- Vmax=0.77 umol/min/mg enzyme with glycine as substrate for acyltransferase activity
- Vmax=223 nmol/min/mg enzyme with arachidoyl-CoA as substrate for acyl-CoA thioesterase activity
Structure
Compartment
Expression
expressed in liver, gallbladder mucosa, pancreas
Pathology
- defects in BAAT are involved in familial hypercholanemia