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EC Tree
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 .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
peroxisomal acyl-coa thioesterase, bile acid-coa thioesterase,
more
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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
peroxisomal acyl-coA thioesterase
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coenzyme A thioesterase 2
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coenzyme A thioesterase 2
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choloyl-CoA + H2O = cholate + CoA
choloyl-CoA + H2O = cholate + CoA
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choloyl-CoA + H2O = cholate + CoA
the catalytic triad is formed by Asp233, Ser255, and Gln305
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choloyl-CoA + H2O = cholate + CoA
the catalytic triad is formed by Asp233, Ser255, and Gln305
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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].
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2-trans-decenoyl-CoA + H2O
2-trans-decenoate + CoA
substrate is a beta-oxidation intermediate, low activity
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?
3-dehydrocholoyl-CoA + H2O
3-dehydrocholate + CoA
3-hydroxypalmitoyl-CoA + H2O
3-hydroxypalmitate + CoA
substrate is a beta-oxidation intermediate, low activity
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?
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
choloyl-CoA + H2O
cholate + CoA
hydroxymethylglutaryl-CoA + H2O
hydroxymethylglutarate + CoA
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?
trihydroxycoprostanoyl-CoA + H2O
trihydroxycoprostanate + CoA
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?
additional information
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3-dehydrocholoyl-CoA + H2O
3-dehydrocholate + CoA
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?
3-dehydrocholoyl-CoA + H2O
3-dehydrocholate + CoA
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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free chenodeoxycholate activates the farnesoid X receptor
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?
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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preferred substrate
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
best substrate
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
best substrate
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?
choloyl-CoA + H2O
cholate + CoA
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enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
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additional information
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no activity with acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA or phenylacetyl-CoA are used as substrates
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additional information
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no activity with acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA or phenylacetyl-CoA are used as substrates
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additional information
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enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
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additional information
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the enzyme has a regulatory function in bile acid metabolism
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additional information
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the enzyme functions as a major regulator of peroxisomal lipid metabolism, the enzyme competes with the bile acid-CoA:amino acid N-acyltranferase for bile acid-CoAs as substrates
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additional information
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the enzyme functions as a major regulator of peroxisomal lipid metabolism, the enzyme competes with the bile acid-CoA:amino acid N-acyltranferase for bile acid-CoAs as substrates
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additional information
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the enzyme shows broad specificity for substrates and (branched) acyl-CoA chain lengths
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additional information
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the enzyme shows broad specificity for substrates and (branched) acyl-CoA chain lengths
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2-trans-decenoyl-CoA + H2O
2-trans-decenoate + CoA
substrate is a beta-oxidation intermediate, low activity
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3-hydroxypalmitoyl-CoA + H2O
3-hydroxypalmitate + CoA
substrate is a beta-oxidation intermediate, low activity
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?
chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
choloyl-CoA + H2O
cholate + CoA
hydroxymethylglutaryl-CoA + H2O
hydroxymethylglutarate + CoA
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?
trihydroxycoprostanoyl-CoA + H2O
trihydroxycoprostanate + CoA
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additional information
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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free chenodeoxycholate activates the farnesoid X receptor
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chenodeoxycholoyl-CoA + H2O
chenodeoxycholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
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choloyl-CoA + H2O
cholate + CoA
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choloyl-CoA + H2O
cholate + CoA
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enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
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additional information
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enzyme is involved in the regulation of free to conjugated bile acid ratio, overview
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additional information
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the enzyme has a regulatory function in bile acid metabolism
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additional information
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the enzyme functions as a major regulator of peroxisomal lipid metabolism, the enzyme competes with the bile acid-CoA:amino acid N-acyltranferase for bile acid-CoAs as substrates
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additional information
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the enzyme functions as a major regulator of peroxisomal lipid metabolism, the enzyme competes with the bile acid-CoA:amino acid N-acyltranferase for bile acid-CoAs as substrates
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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
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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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CoA
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slight inhibition of activity with choloyl-CoA
CoA
product inhibition with regulatory function, 50% inhibition at 0.01-0.015 mM
DTNB
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75% inhibition at 0.3 mM, complete inhibition at 1.3 mM
DTNB
50% inhibition at 0.15 mM
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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
PPARII
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peroxisomal proliferator activated receptor-II activates the enzyme, fibrates are antagonizing the receptor activity
PPARII
peroxisomal proliferator activated receptor-II activates the enzyme, regulatory function, fasting-mediated induction in vivo, dependent on the peroxisomal proliferator WY-14,643
additional information
fasting induces the enzyme
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additional information
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fasting induces the enzyme
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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
0.175
cholyl-CoA
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pH 7.0, 37°C
0.011 - 0.018
dithiothreitol
additional information
additional information
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0.011
dithiothreitol
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pH 8.0, 37°C, with chenodeoxycholoyl-CoA
0.018
dithiothreitol
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pH 8.0, 37°C, with choloyl-CoA
additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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kinetics
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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
0.00227
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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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0.00203
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microsomal fraction of liver homogenate, substrate chenodeoxycholoyl-CoA
0.00203
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mitochondrial fraction of liver homogenate, substrate choloyl-CoA
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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
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4 - 9
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no activity detected below pH 4.0 or above pH 9.0
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brenda
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brenda
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brenda
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SwissProt
brenda
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brenda
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lower enzyme content
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high enzyme content
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lower enzyme content
brenda
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brenda
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brenda
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brenda
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brenda
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healthy and metastatic
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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high activity
brenda
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brenda
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especially in the light mitochondrial fraction
brenda
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brenda
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highest enzyme activity
brenda
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brenda
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brenda
additional information
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subcellular distribution, overview
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brenda
additional information
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multiorganelle distribution, overview
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brenda
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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
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dimer
2 * 35886, amino acid sequence calculation, 2 * 36000, recombinant enzyme, SDS-PAGE
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-20°C, enzyme is stable for several months in 50% glycerol
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partially, subcellular fractionation
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expression in Escherichia coli
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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
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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
brenda
Russell, D.W.
The enzymes, regulation, and genetics of bile acid synthesis
Annu. Rev. Biochem.
72
137-174
2003
Homo sapiens, Mus musculus
brenda
Ye, H.Q.; Mallonee, D.H.; Wells, J.E.; Bjorkhem, I.; Hylemon, P.B.
The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A hydrolase
J. Lipid Res.
40
17-23
1999
Eubacterium sp., Eubacterium sp. VPI 12708
brenda
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
brenda
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
brenda
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