Entry
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
Orthology
K08748 solute carrier family 27 (fatty acid transporter), member 5
K15868 bile acid-coenzyme A ligase
Genes
KIM : G3T16_11475 G3T16_16845
PLA : Plav_1025 Plav_1029 Plav_1034
RBS : RHODOSMS8_00086(baiB)
BCAN : BcanWSM471_03240 BcanWSM471_08330
BXN : I3J27_03165 I3J27_33625 I3J27_33655
VGO : GJW-30_1_02490(baiB_2)
TSV : DSM104635_02995 DSM104635_03075
SMAZ : LH19_12220 LH19_27280
SWI : Swit_0351 Swit_1599 Swit_1600
SPHD : HY78_17585 HY78_17590 HY78_17610 HY78_26355
SJP : SJA_C2-03890 SJA_C2-04050
CSCI : HDCHBGLK_01430(baiB)
PHX : KGNDJEFE_00401(baiB)
MCHI : AN480_08330 AN480_23315 AN480_25245
MMAL : CKJ54_07175 CKJ54_23135
MMAN : MMAN_24730 MMAN_36630
MSER : MTY59_11840 MTY59_33860
MSHG : MSG_00422 MSG_03568
MFJ : MFLOJ_30860 MFLOJ_51280
MSTO : MSTO_34790 MSTO_55390
MSIM : MSIM_20450 MSIM_40770
MKU : I2456_02760 I2456_18740
MLW : MJO58_02270 MJO58_19560
MXE : MYXE_17320 MYXE_46350
MNV : MNVI_02600 MNVI_19750
MPAG : C0J29_02725 C0J29_21705
MGOR : H0P51_02740 H0P51_19675
MCOO : MCOO_16060 MCOO_35900
MBAI : MB901379_03460(lcfB_9)
MSEO : MSEO_23560 MSEO_43170
MHEK : JMUB5695_01801 JMUB5695_04479
MBRD : MBRA_12830 MBRA_32660
MPAA : MKK62_07880 MKK62_23045
MKY : IWGMT90018_04990 IWGMT90018_41340
MWU : PT015_09070 PT015_19535
MYW : BVC93_07035 BVC93_15435
MPHL : MPHLCCUG_04868(baiB_2)
MTHN : 4412656_00248(fadD_2)
MMOR : MMOR_01890 MMOR_58370
MSAL : DSM43276_02035(baiB)
YIA : LO772_03550 LO772_29980 LO772_35175
ACTW : F7P10_09660 F7P10_11280
AMAZ : LUW76_14885 LUW76_14955 LUW76_22035 LUW76_25845
FRE : Franean1_0614 Franean1_4026
FRI : FraEuI1c_2666 FraEuI1c_3335 FraEuI1c_4447 FraEuI1c_5318 FraEuI1c_5444
UME : RM788_00940 RM788_48095
DACT : KZZ52_25735 KZZ52_26285
» show all
Taxonomy
Reference
Authors
ELLIOTT WH.
Title
The enzymic activation of cholic acid by guinea-pig-liver microsomes.
Journal
Reference
Authors
ELLIOTT WH.
Title
The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes.
Journal
Reference
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
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
Reference
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
Sequence
Reference
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
Sequence
Reference
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
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 6.2.1.7
ExPASy - ENZYME nomenclature database: 6.2.1.7
BRENDA, the Enzyme Database: 6.2.1.7
LinkDB
All DBs