BAAT

Bile acid-CoA:amino acid N-acyltransferase is an enzyme that in humans is encoded by the BAAT gene.[5]

BAAT
Identifiers
Aliases	BAAT, BACAT, BAT, bile acid-CoA:amino acid N-acyltransferase
External IDs	OMIM: 602938 MGI: 106642 HomoloGene: 1286 GeneCards: BAAT
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9q31.1 Start 101,360,417 bp[1] End 101,383,519 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 B1|4 26.51 cM Start 49,489,422 bp[2] End 49,506,557 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • thiolester hydrolase activity • very long chain acyl-CoA hydrolase activity • receptor binding • transferase activity • medium-chain acyl-CoA hydrolase activity • hydrolase activity • N-acyltransferase activity • palmitoyl-CoA hydrolase activity • long-chain acyl-CoA hydrolase activity • GO:0004091 carboxylic ester hydrolase activity • glycine N-choloyltransferase activity • GO:0001948 protein binding • transferase activity, transferring acyl groups • myristoyl-CoA hydrolase activity • acyl-CoA hydrolase activity Cellular component • cytoplasm • peroxisome • peroxisomal matrix • cytosol Biological process • bile acid conjugation • liver development • lipid metabolism • animal organ regeneration • acyl-CoA metabolic process • taurine metabolic process • bile acid metabolic process • glycine metabolic process • bile acid biosynthetic process • fatty acid metabolic process • protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	570	12012
Ensembl	ENSG00000136881 ENSG00000276559	ENSMUSG00000039653
UniProt	Q14032	Q91X34
RefSeq (mRNA)	NM_001701 NM_001127610 NM_001374715	NM_007519
RefSeq (protein)	NP_001121082 NP_001692 NP_001361644	NP_031545
Location (UCSC)	Chr 9: 101.36 – 101.38 Mb	Chr 4: 49.49 – 49.51 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene is a liver enzyme that catalyzes the transfer of the bile acid moiety from the acyl-CoA thioester to either glycine or taurine, the second step in the formation of bile acid-amino acid conjugates which serve as detergents in the gastrointestinal tract.[5]

References

1. ENSG00000276559 GRCh38: Ensembl release 89: ENSG00000136881, ENSG00000276559 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000039653 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: BAAT bile acid Coenzyme A: amino acid N-acyltransferase (glycine N-choloyltransferase)".

External links

• Human BAAT genome location and BAAT gene details page in the UCSC Genome Browser.

Further reading

• Johnson MR, Barnes S, Kwakye JB, Diasio RB (1991). "Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver". J. Biol. Chem. 266 (16): 10227–33. PMID 2037576.
• Falany CN, Johnson MR, Barnes S, Diasio RB (1994). "Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase". J. Biol. Chem. 269 (30): 19375–9. PMID 8034703.
• Lench NJ, Telford EA, Andersen SE, et al. (1997). "An EST and STS-based YAC contig map of human chromosome 9q22.3". Genomics. 38 (2): 199–205. doi:10.1006/geno.1996.0616. PMID 8954802.
• Solaas K, Ulvestad A, Söreide O, Kase BF (2000). "Subcellular organization of bile acid amidation in human liver: a key issue in regulating the biosynthesis of bile salts". J. Lipid Res. 41 (7): 1154–62. PMID 10884298.
• Sfakianos MK, Wilson L, Sakalian M, et al. (2003). "Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase". J. Biol. Chem. 277 (49): 47270–5. doi:10.1074/jbc.M207463200. PMID 12239217.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Carlton VE, Harris BZ, Puffenberger EG, et al. (2003). "Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT". Nat. Genet. 34 (1): 91–6. doi:10.1038/ng1147. PMID 12704386.
• Wang H, Tamba M, Kimata M, et al. (2003). "Expression of the activity of cystine/glutamate exchange transporter, system x(c)(-), by xCT and rBAT". Biochem. Biophys. Res. Commun. 305 (3): 611–8. doi:10.1016/S0006-291X(03)00808-8. PMID 12763038.
• O'Byrne J, Hunt MC, Rai DK, et al. (2003). "The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine". J. Biol. Chem. 278 (36): 34237–44. doi:10.1074/jbc.M300987200. PMID 12810727.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Pellicoro A, van den Heuvel FA, Geuken M, et al. (2007). "Human and rat bile acid-CoA:amino acid N-acyltransferase are liver-specific peroxisomal enzymes: implications for intracellular bile salt transport". Hepatology. 45 (2): 340–8. doi:10.1002/hep.21528. PMID 17256745.
• Tougou K, Fukuda T, Ito T, et al. (2007). "Genetic polymorphism of bile acid CoA: amino acid N-acyltransferase in Japanese individuals". Drug Metab. Pharmacokinet. 22 (2): 125–8. doi:10.2133/dmpk.22.125. PMID 17495420.