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Information on EC 6.2.1.7 - cholate-CoA ligase and Organism(s) Homo sapiens

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.7 cholate-CoA ligase
IUBMB Comments
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 . The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 alpha-dehydroxylation pathway .
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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
choloyl-coa synthetase, bile acid:coa ligase, cholic acid:coa ligase, cholate-coa ligase, bile acid-coenzyme a ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bile acid coenzyme A synthetase
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-
-
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Bile acid-coenzyme A ligase
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-
-
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Bile acid:CoA ligase
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-
-
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Cholate thiokinase
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-
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Cholic acid:CoA ligase
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-
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Cholic thiokinase
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-
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Choloyl coenzyme A synthetase
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-
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Choloyl-CoA synthetase
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Synthetase, choloyl coenzyme A
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
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-
SYSTEMATIC NAME
IUBMB Comments
cholate:CoA ligase (AMP-forming)
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9027-90-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + cholate + CoA
AMP + diphosphate + choloyl-CoA
show the reaction diagram
additional information
?
-
-
enzyme additionally activates fatty acids
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + cholate + CoA
AMP + diphosphate + choloyl-CoA
show the reaction diagram
-
re-activation and re-conjugation of bile acids
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
immunohistochemical screening of liver tissue for cholate-CoA ligase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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defects in cholate-CoA ligase and bile acid-CoA:amino acid N-acyltransferase activities can cause intrahepatic cholestasis, overview
physiological function
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cholate-CoA ligase and bile acid-CoA:amino acid N-acyltransferase sequentially mediate bile-acid amidation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
S27A2_HUMAN
620
3
70312
Swiss-Prot
Secretory Pathway (Reliability: 1)
S27A5_HUMAN
690
1
75385
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in COS-1 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Steinberg, S.J.; Mihalik, S.J.; Kim, D.G.; Cuebas, D.A.; Watkins, P.A.
The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate: CoA ligase
J. Biol. Chem.
275
15605-15608
2000
Homo sapiens
Manually annotated by BRENDA team
Hadzic, N.; Bull, L.N.; Clayton, P.T.; Knisely, A.S.
Diagnosis in bile acid-CoA: amino acid N-acyltransferase deficiency
World J. Gastroenterol.
18
3322-3326
2012
Homo sapiens
Manually annotated by BRENDA team