bile acid CoA:amino acid N-acyltransferase (BAT, BACAT, glycine N-choloyltransferase, long-chain fatty-acyl-CoA hydrolase, BAAT)

Function: 1) bile acid metabolism 2) in hepatocytes, catalyzes 2nd step in the conjugation of C24 bile acids (choloneates) to glycine & taurine before excretion into bile canaliculi 3) may catalyze conjugation of primary or secondary bile acids, or both 4) may also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids 5) 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 Kinetic parameters: - 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: monomer Compartment: cytoplasm Expression: expressed in liver, gallbladder mucosa, pancreas Pathology: - defects in BAAT are involved in familial hypercholanemia

Properties

SIZE: MW = 46 kD entity length = 418 aa COMPARTMENT: cytoplasm MOTIF: cysteine residue {C235} aspartate residue {D328} histidine residue {H362}

Database Correlations

OMIM correlations MORBIDMAP 602938 UniProt Q14032 Pfam PF04775 ENZYME correlations

References

UniProt :accession Q14032