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Information on EC 3.1.2.27 - choloyl-CoA hydrolase and Organism(s) Mus musculus and UniProt Accession P58137

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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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Mus musculus
UNIPROT: P58137
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
acyl-CoA thioesterase
-
peroxisomal acyl-coA thioesterase
-
coenzyme A thioesterase 2
-
-
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
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
-
9025-87-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-trans-decenoyl-CoA + H2O
2-trans-decenoate + CoA
show the reaction diagram
substrate is a beta-oxidation intermediate, low activity
-
-
?
3-hydroxypalmitoyl-CoA + H2O
3-hydroxypalmitate + CoA
show the reaction diagram
substrate is a beta-oxidation intermediate, low activity
-
-
?
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
show the reaction diagram
choloyl-CoA + H2O
cholate + CoA
show the reaction diagram
hydroxymethylglutaryl-CoA + H2O
hydroxymethylglutarate + CoA
show the reaction diagram
-
-
-
?
trihydroxycoprostanoyl-CoA + H2O
trihydroxycoprostanate + 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
2-trans-decenoyl-CoA + H2O
2-trans-decenoate + CoA
show the reaction diagram
substrate is a beta-oxidation intermediate, low activity
-
-
?
3-hydroxypalmitoyl-CoA + H2O
3-hydroxypalmitate + CoA
show the reaction diagram
substrate is a beta-oxidation intermediate, low activity
-
-
?
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
show the reaction diagram
-
-
-
?
choloyl-CoA + H2O
cholate + CoA
show the reaction diagram
-
-
-
?
hydroxymethylglutaryl-CoA + H2O
hydroxymethylglutarate + CoA
show the reaction diagram
-
-
-
?
trihydroxycoprostanoyl-CoA + H2O
trihydroxycoprostanate + CoA
show the reaction diagram
-
-
-
?
choloyl-CoA + H2O
cholate + CoA
show the reaction diagram
-
enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
50% inhibition at 0.001 mM
acyl-CoA
enzyme is substrate-inhibited at 0.005-0.01 mM of acyl-CoAs with chain length longer than C10
CoA
product inhibition with regulatory function, 50% inhibition at 0.01-0.015 mM
DTNB
50% inhibition at 0.15 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PPARII
peroxisomal proliferator activated receptor-II activates the enzyme, regulatory function, fasting-mediated induction in vivo, dependent on the peroxisomal proliferator WY-14,643
PPARII
-
peroxisomal proliferator activated receptor-II activates the enzyme, fibrates are antagonizing the receptor activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lower enzyme content
Manually annotated by BRENDA team
high enzyme content
Manually annotated by BRENDA team
lower enzyme content
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOT8_MOUSE
320
0
35827
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35886
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE
36000
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE
70000
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PTE-2, DNA and amino acid sequence determination and analysis, location on chromosome 20q12-q13, expression in Escherichia coli, expression as GFP-fusion protein in human skin fibroblasts showing targeting to the peroxisomes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hunt, M.C.; Solaas, K.; Kase, B.F.; Alexson, S.E.
Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism
J. Biol. Chem.
277
1128-1138
2002
Mus musculus (P58137), Mus musculus
Manually annotated by BRENDA team
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