Names & Taxonomy

Uniprot ID:
Q14032
Entry Name:
BAAT_HUMAN
Status:
reviewed
Protein Names:
Bile acid-CoA:amino acid N-acyltransferase (BACAT) (BAT) (EC 2.3.1.65) (Glycine N-choloyltransferase) (Long-chain fatty-acyl-CoA hydrolase) (EC 3.1.2.2)
Gene Names:
BAAT
Gene Names Primary:
BAAT
Organism:
Homo sapiens (Human)

Structure

Length:
418
Sequence:
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVASAPKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFETTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGAGHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Cytoplasm

Function

Function:
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). 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.
Catalytic Activity:
Choloyl-CoA + glycine = CoA + glycocholate.
Kinetics:
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for taurine toward choloyl-CoA
Active Site:
ACT_SITE 235 235 Charge relay system.
Cross Reference Drug Bank:
DB00145
Gene Ontology Go:
cytosol
peroxisomal matrix
peroxisome
carboxylic ester hydrolase activity
glycine N-choloyltransferase activity
long-chain acyl-CoA hydrolase activity
medium-chain acyl-CoA hydrolase activity
N-acyltransferase activity
palmitoyl-CoA hydrolase activity
receptor binding
very long chain acyl-CoA hydrolase activity
acyl-CoA metabolic process
bile acid and bile salt transport
bile acid biosynthetic process
bile acid conjugation
bile acid metabolic process
fatty acid metabolic process
glycine metabolic process
liver development
organ regeneration
small molecule metabolic process
taurine metabolic process
Gene Ontology Biological Process:
acyl-CoA metabolic process
bile acid and bile salt transport
bile acid biosynthetic process
bile acid conjugation
bile acid metabolic process
fatty acid metabolic process
glycine metabolic process
liver development
organ regeneration
small molecule metabolic process
taurine metabolic process
Gene Ontology Molecular Function:
carboxylic ester hydrolase activity
glycine N-choloyltransferase activity
long-chain acyl-CoA hydrolase activity
medium-chain acyl-CoA hydrolase activity
N-acyltransferase activity
palmitoyl-CoA hydrolase activity
receptor binding
very long chain acyl-CoA hydrolase activity
Gene Ontology Cellular Component:
cytosol
peroxisomal matrix
peroxisome
Keywords:
Acyltransferase
Complete proteome
Cytoplasm
Direct protein sequencing
Disease mutation
Fatty acid metabolism
Hydrolase
Lipid metabolism
Phosphoprotein
Polymorphism
Reference proteome
Serine esterase
Transferase
Interacts With:
Q0D2H9; Q08AF8

Publication

PubMed ID:
8034703 15164053 15489334 2037576 12239217 12810727 24275569 12704386