Information on EC 3.1.2.27 - choloyl-CoA hydrolase

for references in articles please use BRENDA:EC3.1.2.27
Word Map on EC 3.1.2.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.1.2.27
-
RECOMMENDED NAME
GeneOntology No.
choloyl-CoA hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
choloyl-CoA + H2O = cholate + CoA
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Primary bile acid biosynthesis
-
-
Metabolic 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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-dehydrocholoyl-CoA + H2O
3-dehydrocholate + CoA
show the reaction diagram
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
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
P58137
substrate is a beta-oxidation intermediate, low activity
-
-
?
3-hydroxypalmitoyl-CoA + H2O
3-hydroxypalmitate + CoA
show the reaction diagram
P58137
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
P58137
-
-
-
?
trihydroxycoprostanoyl-CoA + H2O
trihydroxycoprostanate + CoA
show the reaction diagram
P58137
-
-
-
?
additional information
?
-
INHIBITORS
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
Phospholipids
-
at high concentrations
additional information
-
substrate competition between choloyl-CoA and chenodeoxycholoyl-CoA, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
-
slight activation of activity with chenodeoxycholoyl-CoA
DTT
-
highly stimulating on the activity with both choloyl-CoA and chenodeoxycholoyl-CoA
PPARII
-
additional information
fasting induces the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.071
chenodeoxycholoyl-CoA
-
pH 8.0, 37°C, postnuclear fraction of liver homogenate
0.077
choloyl-CoA
-
pH 8.0, 37°C, postnuclear fraction of liver homogenate
0.175
cholyl-CoA
-
pH 7.0, 37°C
0.011 - 0.018
DTT
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00118
-
nuclear fraction of liver homogenate, substrate choloyl-CoA
0.00127
-
cytosolic fraction of liver homogenate, substrate choloyl-CoA
0.0014 - 0.0031
-
subcellular fractions, overview
0.00186
-
nuclear fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00203
-
microsomal fraction of liver homogenate, substrate chenodeoxycholoyl-CoA; mitochondrial fraction of liver homogenate, substrate choloyl-CoA
0.00227
-
cytosolic fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00247
-
light mitochondrial fraction of liver homogenate, substrate choloyl-CoA
0.00248
-
microsomal fraction of liver homogenate, substrate choloyl-CoA
0.00263
-
mitochondrial fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00276
-
postnuclear fraction of liver homogenate, substrate choloyl-CoA
0.00297
-
postnuclear fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00334
-
light mitochondrial fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.0133
-
peroxisomal fraction of a metastatic liver homogenate, substrate chenodeoxycholoyl-CoA
0.01602
-
peroxisomal fraction of a metastatic liver homogenate, substrate choloyl-CoA
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
broad optimum with substrate choloyl-CoA
7.4
assay at
7.5 - 9
-
broad optimum with substrate chenodeoxycholoyl-CoA
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 9
-
no activity detected below pH 4.0 or above pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
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
additional information
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme is stable for several months in 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially, subcellular fractionation
-
recombinant
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
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
Show AA Sequence (115 entries)
Please use the Sequence Search for a specific query.