KEGG   ENZYME: 6.2.1.7Help
Entry
EC 6.2.1.7                  Enzyme                                 

Name
cholate---CoA ligase;
BAL;
bile acid CoA ligase;
bile acid coenzyme A ligase;
choloyl-CoA synthetase;
choloyl coenzyme A synthetase;
cholic thiokinase;
cholate thiokinase;
cholic acid:CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl coenzyme A synthetase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate-CoA synthetase;
THCA-CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate---CoA ligase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanate:CoA ligase (AMP-forming);
cholyl-CoA synthetase;
trihydroxycoprostanoyl-CoA synthetase
Class
Ligases;
Forming carbon-sulfur bonds;
Acid-thiol ligases
BRITE hierarchy
Sysname
cholate:CoA ligase (AMP-forming)
Reaction(IUBMB)
(1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA [RN:R02794];
(2) ATP + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA [RN:R04580]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
cholate [CPD:C00695];
CoA [CPD:C00010];
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
choloyl-CoA [CPD:C01794];
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
Comment
Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates [7]. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 alpha-dehydroxylation pathway [5].
History
EC 6.2.1.7 created 1961 (EC 6.2.1.29 created 1992, incorporated 2005), modified 2005
Pathway
ec00120  Primary bile acid biosynthesis
ec00121  Secondary bile acid biosynthesis
ec01100  Metabolic pathways
Orthology
K08748  solute carrier family 27 (fatty acid transporter), member 5
K15868  bile acid-coenzyme A ligase
Genes
HSA: 10998(SLC27A5)
PTR: 456351(SLC27A5)
PPS: 100973518(SLC27A5)
GGO: 101141402(SLC27A5) 109025165
PON: 100450572(SLC27A5)
NLE: 100598523(SLC27A5)
MCC: 713713(SLC27A5)
MCF: 102139611(SLC27A5)
CSAB: 103235458(SLC27A5)
RRO: 104680867(SLC27A5)
RBB: 108514368(SLC27A5)
CJC: 100394591(SLC27A5)
SBQ: 101033269(SLC27A5)
MMU: 26459(Slc27a5)
RNO: 79111(Slc27a5)
CGE: 100765567(Slc27a5)
NGI: 103725476(Slc27a5)
HGL: 101724180(Slc27a5)
CCAN: 109683037(Slc27a5)
OCU: 100340287(SLC27A5)
TUP: 102483776(SLC27A5)
CFA: 484223(SLC27A5) 608675
AML: 100478693(SLC27A5)
UMR: 103677216(SLC27A5)
ORO: 101381954(SLC27A5)
FCA: 101086686(SLC27A5)
PTG: 102948587(SLC27A5)
AJU: 106987933(SLC27A5)
BTA: 533016(SLC27A5)
BOM: 102285844(SLC27A5)
BIU: 109571897(SLC27A5)
PHD: 102331039(SLC27A5)
CHX: 102172839(SLC27A5)
OAS: 101120689(SLC27A5)
SSC: 102158419(SLC27A5)
CFR: 102519177(SLC27A5)
CDK: 105096797(SLC27A5)
BACU: 103020672(SLC27A5)
LVE: 103086085(SLC27A5)
OOR: 101280268(SLC27A5)
ECB: 100051678(SLC27A5)
EPZ: 103567891(SLC27A5)
EAI: 106846663(SLC27A5)
MYB: 102261821(SLC27A5)
MYD: 102751593(SLC27A5)
HAI: 109377097(SLC27A5)
RSS: 109434533(SLC27A5)
PALE: 102890200(SLC27A5)
LAV: 100676206(SLC27A5)
TMU: 101361902
MDO: 100029941(SLC27A5)
SHR: 100916639(SLC27A5)
OAA: 100090562(SLC27A5)
PLA: Plav_1034
RBS: RHODOSMS8_00086(baiB)
BJA: bll0131
BRA: BRADO6529
BBT: BBta_1112
BRS: S23_06710
AOL: S58_10890
VGO: GJW-30_1_02490(baiB_2)
RBM: TEF_16880
CAK: Caul_4604
PZU: PHZ_c2517
RSU: NHU_03725
HNE: HNE_0099(baiB)
SWI: Swit_1599
SPMI: K663_20463
SPHT: K426_28370
MIT: OCO_48560
MIA: OCU_48510
MID: MIP_07342
MYO: OEM_48710
MIR: OCQ_49570
MMC: Mmcs_0223
MKM: Mkms_0233
MJL: Mjls_0213
MMM: W7S_24315
MVA: Mvan_0252
MGI: Mflv_0419
MPHL: MPHLCCUG_04868(baiB_2)
MVQ: MYVA_0257
MTHN: 4412656_00248(fadD_2)
MAB: MAB_2316
MABB: MASS_2242
MCHE: BB28_11610
MSTE: MSTE_02250
SBH: SBI_00137
SEN: SACE_3387(baiB)
PDX: Psed_0542
PSEA: WY02_09705
PSEE: FRP1_04515
PSEH: XF36_02965
KAL: KALB_5626
ELE: Elen_3099
 » show all
Taxonomy
Reference
1  [PMID:13303991]
  Authors
ELLIOTT WH.
  Title
The enzymic activation of cholic acid by guinea-pig-liver microsomes.
  Journal
Biochem J 62:427-33 (1956)
Reference
2  [PMID:13403911]
  Authors
ELLIOTT WH.
  Title
The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes.
  Journal
Biochem J 65:315-21 (1957)
Reference
3  [PMID:3183523]
  Authors
Prydz K, Kase BF, Bjorkhem I, Pedersen JI.
  Title
Subcellular localization of 3 alpha, 7 alpha-dihydroxy- and 3 alpha,7 alpha,12 alpha-trihydroxy-5 beta-cholestanoyl-coenzyme A ligase(s) in rat liver.
  Journal
J Lipid Res 29:997-1004 (1988)
Reference
4  [PMID:2521999]
  Authors
Schepers L, Casteels M, Verheyden K, Parmentier G, Asselberghs S, Eyssen HJ, Mannaerts GP.
  Title
Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver.
  Journal
Biochem J 257:221-9 (1989)
Reference
5  [PMID:1551828]
  Authors
Mallonee DH, Adams JL, Hylemon PB
  Title
The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase.
  Journal
J Bacteriol 174:2065-71 (1992)
DOI:10.1128/JB.174.7.2065-2071.1992
  Sequence
Reference
6  [PMID:9390170]
  Authors
Wheeler JB, Shaw DR, Barnes S.
  Title
Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes.
  Journal
Arch Biochem Biophys 348:15-24 (1997)
DOI:10.1006/abbi.1997.0391
  Sequence
[rno:79111]
Reference
7  [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 43:2062-71 (2002)
  Sequence
[rno:79111]
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.7
IUBMB Enzyme Nomenclature: 6.2.1.7
ExPASy - ENZYME nomenclature database: 6.2.1.7
BRENDA, the Enzyme Database: 6.2.1.7
CAS: 9027-90-1

DBGET integrated database retrieval system