Q63276 · BAAT_RAT
- ProteinBile acid-CoA:amino acid N-acyltransferase
- GeneBaat
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids420 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine (PubMed:12951368, PubMed:624713). More efficient at taurine conjugation of cholyl CoA than glycine conjugation (PubMed:12951368, PubMed:624713). 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 (By similarity).
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 (By similarity).
May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity).
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 (By similarity).
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 (By similarity).
May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity).
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 (By similarity).
Catalytic activity
- choloyl-CoA + glycine = CoA + glycocholate + H+This reaction proceeds in the forward direction.
- eicosanoyl-CoA + H2O = CoA + eicosanoate + H+This reaction proceeds in the forward direction.
- H2O + octadecanoyl-CoA = CoA + H+ + octadecanoateThis reaction proceeds in the forward direction.
- docosanoyl-CoA + H2O = CoA + docosanoate + H+This reaction proceeds in the forward direction.
- H2O + tetracosanoyl-CoA = CoA + H+ + tetracosanoateThis reaction proceeds in the forward direction.
- H2O + hexacosanoyl-CoA = CoA + H+ + hexacosanoateThis reaction proceeds in the forward direction.
- dodecanoyl-CoA + H2O = CoA + dodecanoate + H+This reaction proceeds in the forward direction.
- H2O + tetradecanoyl-CoA = CoA + H+ + tetradecanoateThis reaction proceeds in the forward direction.
- choloyl-CoA + taurine = CoA + H+ + taurocholateThis reaction proceeds in the forward direction.
- chenodeoxycholoyl-CoA + glycine = CoA + glycochenodeoxycholate + H+This reaction proceeds in the forward direction.
- chenodeoxycholoyl-CoA + taurine = CoA + H+ + taurochenodeoxycholateThis reaction proceeds in the forward direction.
- eicosanoyl-CoA + glycine = CoA + H+ + N-eicosanoylglycinateThis reaction proceeds in the forward direction.
- glycine + hexacosanoyl-CoA = CoA + H+ + N-hexacosanoylglycineThis reaction proceeds in the forward direction.
- docosanoyl-CoA + glycine = CoA + H+ + N-docosanoylglycineThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2 mM | taurine toward choloyl-CoA | |||||
4.4 mM | glycine toward choloyl-CoA | |||||
20 μM | glycine toward choloyl-CoA | |||||
10 μM | taurine toward choloyl-CoA | |||||
15 μM | glycine toward deoxycholoyl-CoA | |||||
13 μM | taurine toward deoxycholoyl-CoA | |||||
13 μM | glycine toward chenodeoxycholoyl-CoA | |||||
16 μM | taurine toward chenodeoxycholoyl-CoA | |||||
12 μM | glycine toward lithocholoyl-CoA | |||||
11 μM | taurine toward lithocholoyl-CoA |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
8.69 μmol/min/mg | for glycine toward choloyl-CoA | ||||
4.09 μmol/min/mg | for taurine toward choloyl-CoA | ||||
7.34 μmol/min/mg | for glycine toward deoxycholoyl-CoA | ||||
3.1 μmol/min/mg | for taurine toward deoxycholoyl-CoA | ||||
5.2 μmol/min/mg | for glycine toward chenodeoxycholoyl-CoA | ||||
3.05 μmol/min/mg | for taurine toward chenodeoxycholoyl-CoA | ||||
5.26 μmol/min/mg | for glycine toward lithocholoyl-CoA | ||||
3.42 μmol/min/mg | for taurine toward lithocholoyl-CoA |
pH Dependence
Optimum pH is 7.8.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 235 | Charge relay system | ||||
Sequence: C | ||||||
Active site | 328 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 362 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | peroxisome | |
Molecular Function | carboxylic ester hydrolase activity | |
Molecular Function | choloyl-CoA hydrolase activity | |
Molecular Function | fatty acyl-CoA hydrolase activity | |
Molecular Function | glycine N-choloyltransferase activity | |
Molecular Function | long-chain fatty acyl-CoA hydrolase activity | |
Molecular Function | medium-chain fatty acyl-CoA hydrolase activity | |
Molecular Function | N-acyltransferase activity | |
Molecular Function | very long-chain fatty acyl-CoA hydrolase activity | |
Biological Process | acyl-CoA metabolic process | |
Biological Process | animal organ regeneration | |
Biological Process | bile acid biosynthetic process | |
Biological Process | bile acid conjugation | |
Biological Process | bile acid metabolic process | |
Biological Process | fatty acid metabolic process | |
Biological Process | glycine metabolic process | |
Biological Process | liver development | |
Biological Process | taurine metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBile acid-CoA:amino acid N-acyltransferase
- EC number
- Short namesBACAT; BAT
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ63276
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000202161 | 1-420 | Bile acid-CoA:amino acid N-acyltransferase | |||
Sequence: MAKLTAVPLSALVDEPVHIRVTGLTPFQVVCLQASLKDDKGNLFNSQAFYRASEVGEVDLERDSSLGGDYMGVHPMGLFWSMKPEKLLTRLVKRDVMNRPHKVHIKLCHPYFPVEGKVISSSLDSLILERWYVAPGVTRIHVKEGRIRGALFLPPGEGPFPGVIDLFGGAGGLFEFRASLLASHGFATLALAYWGYDDLPSRLEKVDLEYFEEGVEFLLRHPKVLGPGVGILSVCIGAEIGLSMAINLKQITATVLINGPNFVSSNPHVYRGKVFQPTPCSEEFVTTNALGLVEFYRTFEETADKDSKYCFPIEKAHGHFLFVVGEDDKNLNSKVHAKQAIAQLMKSGKKNWTLLSYPGAGHLIEPPYSPLCSASRMPFVIPSINWGGEVIPHAAAQEHSWKEIQKFLKQHLNPGFNSQL | ||||||
Modified residue | 40 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 125 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 346 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 350 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 409 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 418 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in liver (at protein level); found in hepatocytes, sinusoidal endothelial cells and Kupffer cells.
Gene expression databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length420
- Mass (Da)46,465
- Last updated2005-11-08 v2
- ChecksumAACDB03726EB546F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 133 | in Ref. 1; BAA07901 | ||||
Sequence: V → M |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D43964 EMBL· GenBank· DDBJ | BAA07901.1 EMBL· GenBank· DDBJ | mRNA | ||
BC088153 EMBL· GenBank· DDBJ | AAH88153.1 EMBL· GenBank· DDBJ | mRNA |