| glycine N-choloyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.3.1.65 | ||||||||
| CAS no. | 74506-32-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a bile acid-CoA:amino acid N-acyltransferase (EC 2.3.1.65) is an enzyme that catalyzes the chemical reaction
- choloyl-CoA + glycine CoA + glycocholate
Thus, the two substrates of this enzyme are choloyl-CoA and glycine, whereas its two products are CoA and glycocholate.
This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is choloyl-CoA:glycine N-choloyltransferase. Other names in common use include glycine-taurine N-acyltransferase, amino acid N-choloyltransferase, BAT, glycine N-choloyltransferase, BACAT, cholyl-CoA glycine-taurine N-acyltransferase, and cholyl-CoA:taurine N-acyltransferase. This enzyme participates in bile acid biosynthesis and taurine and hypotaurine metabolism.
References[edit]
- Czuba B, Vessey DA (1980). "Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver". J. Biol. Chem. 255 (11): 5296–9. PMID 7372637.
- Jordan TW, Lee R, Lim WC (1980). "Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver". Biochem. Int. 1: 325–330.
- Vessey DA (1979). "The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver". J. Biol. Chem. 254 (6): 2059–63. PMID 422567.
- 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, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S (2002). "Molecular cloning and expression of rat liver bile acid CoA ligase". J. Lipid Res. 43 (12): 2062–71. doi:10.1194/jlr.M200260-JLR200. PMID 12454267.
- He D, Barnes S, Falany CN (2003). "Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization". J. Lipid Res. 44 (12): 2242–9. doi:10.1194/jlr.M300128-JLR200. PMID 12951368.
- O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE (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.
