Enzyme

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     6. Ligases
        6.2 Forming carbon-sulfur bonds
            6.2.1 Acid-thiol ligases
ID:6.2.1.7
Description:Cholate--CoA ligase.
Alternative Name: Trihydroxycoprostanoyl-CoA synthetase.
THCA-CoA ligase.
Cholyl-CoA synthetase.
Choloyl-CoA synthetase.
Choloyl coenzyme A synthetase.
Cholic thiokinase.
Cholic acid:CoA ligase.
Cholate thiokinase.
Bile acid coenzyme A ligase.
Bile acid CoA ligase.
BAL.
synthetase.
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl coenzyme A
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA synthetase.
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoate-CoA ligase.
forming).
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate:CoA ligase (AMP-
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate--CoA ligase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.2.1.7
BRENDA Enzyme Link: BRENDA 6.2.1.7
KEGG Enzyme Link: KEGG6.2.1.7
BioCyc Enzyme Link: BioCyc 6.2.1.7
ExPASy Enzyme Link: ExPASy6.2.1.7
EC2PDB Enzyme Link: EC2PDB 6.2.1.7
ExplorEnz Enzyme Link: ExplorEnz 6.2.1.7
PRIAM enzyme-specific profiles Link: PRIAM 6.2.1.7
IntEnz Enzyme Link: IntEnz 6.2.1.7
MEDLINE Enzyme Link: MEDLINE 6.2.1.7
MSA:

6.2.1.7;

Phylogenetic Tree:

6.2.1.7;

Uniprot:
M-CSA:
RHEA:23532 ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate
RULE(radius=1) [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[SH;+0:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:6]-[OH;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:12].[*:7]-[S;H0;+0:8]-[C;H0;+0:10](=[*:9])-[*:11]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Molecular cloning and expression of rat liver bile acid CoA ligase.Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S2002 Dec12454267
Determination of the mechanism of reaction for bile acid: CoA ligase.Kelley M, Vessey DA1994 Dec 157818501
Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain catabolism.Casabon I, Swain K, Crowe AM, Eltis LD, Mohn WW2014 Feb24244004
The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase.Mallonee DH, Adams JL, Hylemon PB1992 Apr1551828
Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling.Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA2002 Jul 511980911

RHEA:22976 (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + ATP + CoA = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + AMP + diphosphate
RULE(radius=1) [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[SH;+0:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:6]-[OH;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:12].[*:9]=[C;H0;+0:10](-[*:11])-[S;H0;+0:8]-[*:7]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Molecular cloning and expression of rat liver bile acid CoA ligase.Falany CN, Xie X, Wheeler JB, Wang J, Smith M, He D, Barnes S2002 Dec12454267
Determination of the mechanism of reaction for bile acid: CoA ligase.Kelley M, Vessey DA1994 Dec 157818501
Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling.Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA2002 Jul 511980911