KEGG   ENZYME: 2.3.1.65Help
Entry
EC 2.3.1.65                 Enzyme                                 

Name bile acid-CoA:amino acid N-acyltransferase;
glycine---taurine N-acyltransferase;
amino acid N-choloyltransferase;
BAT;
glycine N-choloyltransferase;
BACAT;
cholyl-CoA glycine-taurine N-acyltransferase;
cholyl-CoA:taurine N-acyltransferase
Class Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname choloyl-CoA:glycine N-choloyltransferase
Reaction(IUBMB) choloyl-CoA + glycine = CoA + glycocholate [RN:R03718]
Reaction(KEGG) R03718;
(other) R03720 R08744 R08745
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Substrate choloyl-CoA [CPD:C01794];
glycine [CPD:C00037]
Product CoA [CPD:C00010];
glycocholate [CPD:C01921]
Comment Also acts on CoA derivatives of other bile acids. Taurine and
2-fluoro-beta-alanine can act as substrates, but more slowly [4].
The enzyme can also conjugate fatty acids to glycine and can act as
a very-long-chain acyl-CoA thioesterase [7]. Bile-acid---amino-acid
conjugates serve as detergents in the gastrointestinal tract,
solubilizing long chain fatty acids, mono- and diglycerides,
fat-soluble vitamins and cholesterol [4]. This is the second enzyme
in a two-step process leading to the conjugation of bile acids with
amino acids; the first step is the conversion of bile acids into
their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7,
cholate---CoA ligase.
Pathway PATH: ec00120  Primary bile acid biosynthesis
PATH: ec00430  Taurine and hypotaurine metabolism
PATH: ec01100  Metabolic pathways
Orthology KO: K00659  bile acid-CoA:amino acid N-acyltransferase
Genes HSA: 570(BAAT)
MCC: 713983
MMU: 12012(Baat)
RNO: 29725(Baat)
CFA: 481635(BAAT)
BTA: 530653
ECB: 100054567(BAAT)
MDO: 100023136
XLA: 100137716
XTR: 100125079
Taxonomy
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:7372637]
Czuba B, Vessey DA.
Kinetic characterization of cholyl-CoA glycine-taurine
N-acyltransferase from bovine liver.
J. Biol. Chem. 255 (1980) 5296-9.
Bos taurus [GN:bta]
Reference
  Authors
  Title

  Journal
2
Jordan, T.W., Lee, R. and Lim, W.C.
Isoelectric focussing of soluble and particulate benzoyl-CoA and
cholyl-CoA:amino acid N-acyltransferases from rat liver.
Biochem. Int. 1 (1980) 325-330.
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:422567]
Vessey DA.
The co-purification and common identity of cholyl CoA:glycine- and
cholyl CoA:taurine-N-acyltransferase activities from bovine liver.
J. Biol. Chem. 254 (1979) 2059-63.
Bos taurus [GN:bta]
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:2037576]
Johnson MR, Barnes S, Kwakye JB, Diasio RB.
Purification and characterization of bile acid-CoA:amino acid
N-acyltransferase from human liver.
J. Biol. Chem. 266 (1991) 10227-33.
Homo sapiens [GN:hsa]
Reference
  Authors
  Title
  Journal
  Organism
5  [PMID:12454267]
Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S.
Molecular cloning and expression of rat liver bile acid CoA ligase.
J. Lipid. Res. 43 (2002) 2062-71.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
6  [PMID:12951368]
He D, Barnes S, Falany CN.
Rat liver bile acid CoA:amino acid N-acyltransferase: expression,
characterization, and peroxisomal localization.
J. Lipid. Res. 44 (2003) 2242-9.
Rattus norvegicus [GN:rno]
Reference
  Authors
  Title

  Journal
  Organism
7  [PMID:12810727]
O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE.
The human bile acid-CoA:amino acid N-acyltransferase functions in
the conjugation of fatty acids to glycine.
J. Biol. Chem. 278 (2003) 34237-44.
Homo sapiens [GN:hsa]
Other DBs ExplorEnz - The Enzyme Database: 2.3.1.65
IUBMB Enzyme Nomenclature: 2.3.1.65
ExPASy - ENZYME nomenclature database: 2.3.1.65
BRENDA, the Enzyme Database: 2.3.1.65
CAS: 65979-40-0

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