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EC Tree
IUBMB Comments Requires ATP. The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration . However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate and not via hydration of a 24(25) double bond . In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate .
The enzyme appears in viruses and cellular organisms
Synonyms
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, THC-CoA oxidase, THCA-CoA oxidase, THCCox, Trihydroxycoprostanoyl-CoA oxidase,
more
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
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Trihydroxycoprostanoyl-CoA oxidase
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
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THC-CoA oxidase
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THCA-CoA oxidase
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Trihydroxycoprostanoyl-CoA oxidase
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Trihydroxycoprostanoyl-CoA oxidase
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Trihydroxycoprostanoyl-CoA oxidase
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(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
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oxidation
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redox reaction
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reduction
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(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:acceptor 24-oxidoreductase (24R-hydroxylating)
Requires ATP. The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration [1]. However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate and not via hydration of a 24(25) double bond [5]. In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate [1].
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(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor
(24R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
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the 25S epimer is a preferential substrate
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(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
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(25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA + H2O + acceptor
(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-en-27-oic acid + reduced acceptor
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no activity with (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA
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2-methylhexanoyl-CoA + H2O + acceptor
3-hydroxy-2-methylhexanoyl-CoA + reduced acceptor
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2-methylpalmitoyl-CoA + H2O + acceptor
3-hydroxy-2-methylhexandecanoyl-CoA + reduced acceptor
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA + reduced acceptor
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conversion of the coenzyme A ester is lower than with the free acid as substrate
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3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoic acid + reduced acceptor
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pristanoyl-CoA + H2O + acceptor
3-hydroxy-1,6,10,14-tetramethylpentadecanoyl-CoA + reduced acceptor
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trihydroxycoprostanoyl-CoA + H2O + acceptor
3alpha,7alpha,12alpha,24-tetrahydroxycoprostanoyl-CoA + reduced acceptor
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additional information
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noninducible enzyme
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additional information
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noninducible enzyme
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coenzyme A
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marked inhibition of reaction with 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid
FAD
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contains most likely 2 mol of loosely bound FAD per mol of enzyme
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(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA
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additional information
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oxygen may be obligatory since there is almost complete inhibition when the reaction is performed in an atmosphere consisting of nitrogen
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1,2-Butanediol
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activates
1,2-propanediol
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activates
1,3-Propanediol
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activates
2,3-Butanediol
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activates
GTP
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stimulates to a lesser degree than ATP
ITP
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stimulates to a lesser degree than ATP
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additional information
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6.5 - 8.5
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pH 6.5: about 30% of maximal activity, pH 8.5: about 60% of maximal activity
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brenda
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SwissProt
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Swissprot
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ACOX2_HUMAN
681
0
76827
Swiss-Prot
other Location (Reliability: 4 )
ACOX2_MOUSE
681
0
76863
Swiss-Prot
other Location (Reliability: 2 )
ACOX2_RABIT
681
0
76199
Swiss-Prot
other Location (Reliability: 5 )
ACOX2_RAT
681
0
76799
Swiss-Prot
other Location (Reliability: 3 )
A0A061II13_CRIGR
837
0
94619
TrEMBL
other Location (Reliability: 3 )
A0A061IPB3_CRIGR
1245
1
140876
TrEMBL
other Location (Reliability: 3 )
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175000
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non-denaturing PAGE
68800
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2 * 68800, SDS-PAGE
69000
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2 * 69000, SDS-PAGE
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dimer
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2 * 69000, SDS-PAGE
dimer
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2 * 68800, SDS-PAGE
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in presence of dithiothreitol, the enzyme is very stable in high concentrations of ethylene glycol,1,2-propanediol, 1,3-propanediol, 1,2-butanediol, 2,3-butanediol and 1,3-butanediol, 40-60 v/v
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1,2-butanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
1,2-propanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
1,3-butanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
1,3-propanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
2,3-butanediol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
Ethylene glycol
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40-60 v/v, in presence of dithiothreitol, the enzyme is very stable
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partial
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Schepers, L.; Van Veldhoven, P.P.; Casteels, M.; Eyssen, H.J.; Mannaerts, G.P.
Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase
J. Biol. Chem.
265
5242-5246
1990
Rattus norvegicus
brenda
Pedersen, J.I.; Veggan, T.; Bjorkhem, I.
Substrate stereospecificity in oxidation of (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA by peroxisomal trihydroxy-5beta-cholestanoyl-CoA oxidase
Biochem. Biophys. Res. Commun.
224
37-42
1996
Oryctolagus cuniculus
brenda
van Veldhoven, P.P.; van Rompuy, P.; Vanhooren, J.C.; Mannaerts, G.P.
Purification and further characterization of peroxisomal trihydroxycoprostanoyl-CoA oxidase from rat liver
Biochem. J.
304
195-200
1994
Rattus norvegicus
brenda
Baumgart, E.; Vanhooren, J.C.; Fransen, M.; van Leuven, F.; Fahimi, H.D.; van Veldhoven, P.P.; Mannaerts, G.P.
Molecular cloning and further characterization of rat peroxisomal trihydroxycoprostanoyl-CoA oxidase
Biochem. J.
320
115-121
1996
Rattus norvegicus (P97562)
brenda
Dieuaide-Noubhani, M.; Novikov, D.; Baumgart, E.; Vanhooren, J.C.T.; Fransen, M.; Goethals, M.; Vanderkerckhove, J.; van Veldhoven, P.P.; Mannaerts, G.P.
Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins
Eur. J. Biochem.
240
660-666
1996
Rattus norvegicus
brenda
van Veldhoven, P.P.; Croes, K.; Asselberghs, S.; Herdewijn, P.; Mannaerts, G.P.
Peroxisomal beta-oxidation of 2-methyl-branched acyl-CoA esters: stereospecific recognition of the 2S-methyl compounds by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase
FEBS Lett.
388
80-84
1996
Rattus norvegicus
brenda
Gustafsson, J.
Biosynthesis of cholic acid in rat liver. 24-Hydroxylation of 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid
J. Biol. Chem.
250
8243-8247
1975
Rattus norvegicus
brenda
Casteels, M.; Schepers, L.; Van Eldere, J.; Eyssen, H.J.; Mannaerts, G.P.
Inhibition of 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid oxidation and of bile acid secretion in rat liver by fatty acids
J. Biol. Chem.
263
4654-4661
1988
Rattus norvegicus
brenda
Van Veldhoven, P.P.; Vanhove, G.; Assselberghs, S.; Eyssen, H.J.; Mannaerts, G.P.
Substrate specificities of rat liver peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase
J. Biol. Chem.
267
20065-20074
1992
Rattus norvegicus
brenda
Pedersen, J.I.; Eggertsen, G.; Hellman, U.; Andersson, U.; Bjorkhem, I.
Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase from rabbit liver
J. Biol. Chem.
272
18481-18489
1997
Oryctolagus cuniculus (O02767)
brenda
Casteels, M.; Schepers, L.; Van Veldhoven, P.P.; Eyssen, H.J.; Mannaerts, G.P.
Separate peroxisomal oxidases for fatty acyl-CoAs and trihydroxycoprostanoyl-CoA in human liver
J. Lipid Res.
31
1865-1872
1990
Homo sapiens
brenda
Ikegawa, S.; Goto, T.; Mano, N.; Goto, J.
Substrate specificity of THCA-CoA oxidases from rat liver light mitochondrial fractions on dehydrogenation of 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid CoA thioester
Steroids
63
603-607
1998
Rattus norvegicus
brenda
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