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Information on EC 3.1.2.27 - choloyl-CoA hydrolase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.2 Thioester hydrolases
                3.1.2.27 choloyl-CoA hydrolase
IUBMB Comments
Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short- and medium- to long-chain acyl-CoAs, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoAs, all of which are present in peroxisomes. The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome .
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This record set is specific for:
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: Bacteria, Eukaryota
Reaction Schemes
Synonyms
peroxisomal acyl-coa thioesterase, bile acid-coa thioesterase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bile acid-CoA thioesterase
-
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chenodeoxycholic acid-CoA thioesterase
-
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chenodeoxycholoyl-coenzyme A thioesterase
-
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choloyl-coenzyme A thioesterase
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coenzyme A thioesterase 2
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
choloyl-CoA + H2O = cholate + CoA
show the reaction diagram
the catalytic triad is formed by Asp233, Ser255, and Gln305
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
choloyl-CoA hydrolase
Also acts on chenodeoxycholoyl-CoA and to a lesser extent on short- and medium- to long-chain acyl-CoAs, and other substrates, including trihydroxycoprostanoyl-CoA, hydroxymethylglutaryl-CoA and branched chain acyl-CoAs, all of which are present in peroxisomes. The enzyme is strongly inhibited by CoA and may be involved in controlling CoA levels in the peroxisome [1].
CAS REGISTRY NUMBER
COMMENTARY hide
37270-64-7
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9025-87-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
show the reaction diagram
choloyl-CoA + H2O
cholate + CoA
show the reaction diagram
additional information
?
-
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
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
show the reaction diagram
choloyl-CoA + H2O
cholate + CoA
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
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slight inhibition of activity with choloyl-CoA
DTNB
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75% inhibition at 0.3 mM, complete inhibition at 1.3 mM
Phospholipids
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at high concentrations
additional information
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substrate competition between choloyl-CoA and chenodeoxycholoyl-CoA, overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
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slight activation of activity with chenodeoxycholoyl-CoA
DTT
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highly stimulating on the activity with both choloyl-CoA and chenodeoxycholoyl-CoA
PPARII
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peroxisomal proliferator activated receptor-II activates the enzyme, fibrates are antagonizing the receptor activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.071
chenodeoxycholoyl-CoA
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pH 8.0, 37°C, postnuclear fraction of liver homogenate
0.077
choloyl-CoA
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pH 8.0, 37°C, postnuclear fraction of liver homogenate
0.011 - 0.018
dithiothreitol
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00118
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nuclear fraction of liver homogenate, substrate choloyl-CoA
0.00127
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cytosolic fraction of liver homogenate, substrate choloyl-CoA
0.0014 - 0.0031
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subcellular fractions, overview
0.00186
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nuclear fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00203
0.00227
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cytosolic fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00247
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light mitochondrial fraction of liver homogenate, substrate choloyl-CoA
0.00248
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microsomal fraction of liver homogenate, substrate choloyl-CoA
0.00263
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mitochondrial fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00276
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postnuclear fraction of liver homogenate, substrate choloyl-CoA
0.00297
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postnuclear fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00334
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light mitochondrial fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.0133
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peroxisomal fraction of a metastatic liver homogenate, substrate chenodeoxycholoyl-CoA
0.01602
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peroxisomal fraction of a metastatic liver homogenate, substrate choloyl-CoA
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
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broad optimum with substrate choloyl-CoA
7.5 - 9
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broad optimum with substrate chenodeoxycholoyl-CoA
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOT8_HUMAN
319
0
35914
Swiss-Prot
other Location (Reliability: 2)
BAAT_HUMAN
418
0
46299
Swiss-Prot
other Location (Reliability: 3)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially, subcellular fractionation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Russell, D.W.
The enzymes, regulation, and genetics of bile acid synthesis
Annu. Rev. Biochem.
72
137-174
2003
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Solaas, K.; Ulvestad, A.; Soreide, O.; Kase, B.F.
Subcellular organization of bile acid amidation in human liver: a key issue in regulating the biosynthesis of bile salts
J. Lipid Res.
41
1154-1162
2000
Homo sapiens
Manually annotated by BRENDA team
Solaas, K.; Sletta, R.J.; Soreide, O.; Kase, B.F.
Presence of choloyl- and chenodeoxycholoyl-coenzyme A thioesterase activity in human liver
Scand. J. Clin. Lab. Invest.
60
91-102
2000
Homo sapiens
Manually annotated by BRENDA team