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)
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.
History
EC 2.3.1.65 created 1983, modified 2005
Pathway
Primary bile acid biosynthesis
Taurine and hypotaurine metabolism
Metabolic pathways
Orthology
K00659  
bile acid-CoA:amino acid N-acyltransferase
Genes
HSA: 
570(BAAT)
PTR: 
472997(BAAT)
PPS: 
100992429(BAAT)
GGO: 
101140183(BAAT)
PON: 
100431907(BAAT)
MCC: 
100429419(BAAT)
MCF: 
102132073(BAAT)
MMU: 
12012(Baat)
RNO: 
29725(Baat)
CGE: 
100756252(Baat)
HGL: 
TUP: 
CFA: 
481635(BAAT)
AML: 
FCA: 
PTG: 
102969591(BAAT)
BTA: 
BOM: 
PHD: 
CHX: 
OAS: 
SSC: 
CFR: 
BACU: 
LVE: 
ECB: 
100054567(BAAT)
MYB: 
MYD: 
PALE: 
MDO: 
100023136(BAAT)
SHR: 
GGA: 
769879(BAAT)
MGP: 
TGU: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
CMY: 
ACS: 
100566890(baat)
PBI: 
XLA: 
XTR: 
TRU: 
OLA: 
XMA: 
LCM: 
BFO: 
CIN: 
 » show all
Taxonomy
Reference
1  [PMID:7372637]
  Authors
Czuba B, Vessey DA.
  Title
Kinetic characterization of cholyl-CoA glycine-taurine N-acyltransferase from bovine liver.
  Journal
J. Biol. Chem. 255 (1980) 5296-9.
Reference
2
  Authors
Jordan, T.W., Lee, R. and Lim, W.C.
  Title
Isoelectric focussing of soluble and particulate benzoyl-CoA and cholyl-CoA:amino acid N-acyltransferases from rat liver.
  Journal
Biochem. Int. 1 (1980) 325-330.
Reference
3  [PMID:422567]
  Authors
Vessey DA.
  Title
The co-purification and common identity of cholyl CoA:glycine- and cholyl CoA:taurine-N-acyltransferase activities from bovine liver.
  Journal
J. Biol. Chem. 254 (1979) 2059-63.
Reference
4  [PMID:2037576]
  Authors
Johnson MR, Barnes S, Kwakye JB, Diasio RB.
  Title
Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver.
  Journal
J. Biol. Chem. 266 (1991) 10227-33.
  Sequence
[hsa:570]
Reference
5  [PMID:12454267]
  Authors
Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S.
  Title
Molecular cloning and expression of rat liver bile acid CoA ligase.
  Journal
J. Lipid. Res. 43 (2002) 2062-71.
Reference
6  [PMID:12951368]
  Authors
He D, Barnes S, Falany CN.
  Title
Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization.
  Journal
J. Lipid. Res. 44 (2003) 2242-9.
  Sequence
[rno:29725]
Reference
7  [PMID:12810727]
  Authors
O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE.
  Title
The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine.
  Journal
J. Biol. Chem. 278 (2003) 34237-44.
  Sequence
[hsa:570]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
65979-40-0

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