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Information on EC 1.17.99.3 - 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC1.17.99.3
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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 .
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
THC-CoA oxidase
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Trihydroxycoprostanoyl-CoA oxidase
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(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].
CAS REGISTRY NUMBER
COMMENTARY hide
119799-47-2
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152787-68-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
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-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOX2_HUMAN
681
0
76827
Swiss-Prot
other Location (Reliability: 4)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team