|Gene:||POR||Accession Number: G-10911 (MetaCyc)|
Species: Oryctolagus cuniculus
Component of: 7α-hydroxycholest-4-en-3-one 12α-hydroxylase
The enzyme is believed to form a stable, 1:1 complex with cytochrome P450 (in [Black82]).
The native apparent molecular mass was determined by SDS-PAGE [Black82].
Gene Citations: [Katagiri86]
Molecular Weight of Polypeptide: 76.588 kD (from nucleotide sequence), 77.0 kD (experimental) [Black82 ]
Relationship Links: Entrez-Nucleotide:PART-OF:D00101 , InterPro:IN-FAMILY:IPR001094 , InterPro:IN-FAMILY:IPR001433 , InterPro:IN-FAMILY:IPR001709 , InterPro:IN-FAMILY:IPR003097 , InterPro:IN-FAMILY:IPR008254 , InterPro:IN-FAMILY:IPR017927 , InterPro:IN-FAMILY:IPR017938 , InterPro:IN-FAMILY:IPR023173 , InterPro:IN-FAMILY:IPR023208 , InterPro:IN-FAMILY:IPR029039 , Pfam:IN-FAMILY:PF00175 , Pfam:IN-FAMILY:PF00258 , Pfam:IN-FAMILY:PF00667 , Prints:IN-FAMILY:PR00369 , Prints:IN-FAMILY:PR00371 , Prosite:IN-FAMILY:PS50902 , Prosite:IN-FAMILY:PS51384
Enzymatic reaction of: NADPH-cytochrome P450 reductase
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Reversibility of this reaction is unspecified.
Cytochrome b5 is also reduced by this enzyme (in [Black82]).
Subunit of: 7α-hydroxycholest-4-en-3-one 12α-hydroxylase
Species: Oryctolagus cuniculus
Subunit composition of
7α-hydroxycholest-4-en-3-one 12α-hydroxylase = [POR][CYP8B1]
NADPH-cytochrome P450 reductase = POR (summary available)
cytochrome P450 8B1 = CYP8B1 (summary available)
Enzymatic reaction of: 7α-hydroxycholest-4-en-3-one 12α-hydroxylase
Synonyms: 7α-hydroxy-4-cholesten-3-one 12α-hydroxylase, sterol 12α-hydroxylase, 7α-hydroxy-4-cholesten-3-one 12α-monooxygenase, 7α-hydroxycholest-4-en-3-one,NADPH:oxygen oxidoreductase (12α-hydroxylating)
EC Number: 126.96.36.199
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: bile acid biosynthesis, neutral pathway
This enzyme requires NADPH-cytochrome P450 reductase for its activity. It was assayed using the reductase, phospholipid and a NADPH regenerating system. Inclusion of cytochrome b5 enhanced the activity [Ishida92].
The level of this enzyme activity determines the relative amounts of cholate and chenodeoxycholate (or other species-specific bile acid) produced in the liver. The 12α hydroxylation leads to cholate biosynthesis (reviewed in [Russell03] and [Norlin07]).
This enzyme also catalyzes EC 188.8.131.52 (5β-cholestane-3α,7α-diol + NAD(P)H + oxygen + H+ → 5β-cholestane-3α,7α,12α-triol + NAD(P)+ + H2O) and has broad substrate specificity, although 7α-hydroxycholest-4-en-3-one was the more efficient substrate. Recombinant enzyme was also demonstrated to have these activities [Andersson98].
Andersson98: Andersson U, Eggertsen G, Bjorkhem I (1998). "Rabbit liver contains one major sterol 12alpha-hydroxylase with broad substrate specificity." Biochim Biophys Acta 1389(2);150-4. PMID: 9461256
Black82: Black SD, Coon MJ (1982). "Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region." J Biol Chem 257(10);5929-38. PMID: 6802823
Katagiri86: Katagiri M, Murakami H, Yabusaki Y, Sugiyama T, Okamoto M, Yamano T, Ohkawa H (1986). "Molecular cloning and sequence analysis of full-length cDNA for rabbit liver NADPH-cytochrome P-450 reductase mRNA." J Biochem 100(4);945-54. PMID: 3029050
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493