KEGG   ENZYME: 1.17.99.3Help
Entry
EC 1.17.99.3                Enzyme                                 

Name
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase;
trihydroxycoprostanoyl-CoA oxidase;
THC-CoA oxidase;
THCA-CoA oxidase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase;
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase
Class
Oxidoreductases;
Acting on CH or CH2 groups;
With other, unknown, acceptors
BRITE hierarchy
Sysname
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:acceptor 24-oxidoreductase (24R-hydroxylating)
Reaction(IUBMB)
(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 [RN:R07374]
Reaction(KEGG)
R07374;
(other) R08735 R08740
Show
Substrate
(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA [CPD:C15613];
H2O [CPD:C00001];
acceptor [CPD:C00028]
Product
(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA [CPD:C15614];
reduced acceptor [CPD:C00030]
Comment
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].
History
EC 1.17.99.3 created 2005
Pathway
Primary bile acid biosynthesis
Metabolic pathways
Orthology
K10214  
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase
Genes
HSA: 
8309(ACOX2)
PTR: 
460479(ACOX2)
PPS: 
100987633(ACOX2)
GGO: 
101135855(ACOX2)
PON: 
100173031(ACOX2)
MCC: 
701565(ACOX2)
MCF: 
102142571(ACOX2)
MMU: 
93732(Acox2)
RNO: 
252898(Acox2)
CGE: 
100766043(Acox2)
HGL: 
101716015(Acox2)
TUP: 
102491187(ACOX2)
CFA: 
100855488(ACOX2)
AML: 
100483316(ACOX2)
FCA: 
101101039(ACOX2)
PTG: 
102972085(ACOX2)
BTA: 
514969(ACOX2)
BOM: 
102287053(ACOX2)
PHD: 
102318717(ACOX2)
CHX: 
102184385(ACOX2)
OAS: 
101121460(ACOX2)
SSC: 
100516877(ACOX2)
CFR: 
102512694(ACOX2)
BACU: 
102999785(ACOX2)
LVE: 
103086040(ACOX2)
ECB: 
100050425(ACOX2)
MYB: 
102260512(ACOX2)
MYD: 
102766328(ACOX2)
PALE: 
102884254(ACOX2)
MDO: 
100028782(ACOX2)
SHR: 
100924634(ACOX2)
OAA: 
100074731(ACOX2)
GGA: 
416068(ACOX2)
MGP: 
100545690(ACOX2)
TGU: 
100228411(ACOX2)
FAB: 
101820029(ACOX2)
PHI: 
102102070(ACOX2)
APLA: 
101804343(ACOX2)
FPG: 
101910731(ACOX2)
FCH: 
102048175(ACOX2)
CLV: 
102092775(ACOX2)
ASN: 
102380977(ACOX2)
AMJ: 
102563802(ACOX2)
PSS: 
102450027(ACOX2)
CMY: 
102935400(ACOX2)
ACS: 
100556696(acox2)
PBI: 
103062545(ACOX2)
XLA: 
414480(acox2)
XTR: 
548740(acox2)
LCM: 
102363316(ACOX2)
CMK: 
103179753(acox2)
CIN: 
100186223(acox2)
 » show all
Taxonomy
Reference
1  [PMID:240854]
  Authors
Gustafsson J.
  Title
Biosynthesis of cholic acid in rat liver. 24-Hydroxylation of 3alpha, 7alpha, 12alpha-trihydroxy-5beta-cholestanoic acid.
  Journal
J. Biol. Chem. 250 (1975) 8243-7.
Reference
2  [PMID:2156865]
  Authors
Schepers L, Van Veldhoven PP, Casteels M, Eyssen HJ, Mannaerts GP.
  Title
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.
  Journal
J. Biol. Chem. 265 (1990) 5242-6.
Reference
3  [PMID:8856068]
  Authors
Dieuaide-Noubhani M, Novikov D, Baumgart E, Vanhooren JC, Fransen M, Goethals M, Vandekerckhove J, Van Veldhoven PP, Mannaerts GP.
  Title
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.
  Journal
Eur. J. Biochem. 240 (1996) 660-6.
Reference
4  [PMID:8856068]
  Authors
Dieuaide-Noubhani M, Novikov D, Baumgart E, Vanhooren JC, Fransen M, Goethals M, Vandekerckhove J, Van Veldhoven PP, Mannaerts GP.
  Title
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.
  Journal
Eur. J. Biochem. 240 (1996) 660-6.
Reference
5  [PMID:9218493]
  Authors
Pedersen JI, Eggertsen G, Hellman U, Andersson U, Bjorkhem I.
  Title
Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-trihydroxy-5beta-chole stanoyl-CoA oxidase from rabbit liver.
  Journal
J. Biol. Chem. 272 (1997) 18481-9.
  Sequence
[up:O02767]
Reference
6  [PMID:12543708]
  Authors
Russell DW.
  Title
The enzymes, regulation, and genetics of bile acid synthesis.
  Journal
Annu. Rev. Biochem. 72 (2003) 137-74.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
119799-47-2

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