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Literature summary for 1.14.14.17 extracted from

  • Li, L.; Porter, T.D.
    Hepatic cytochrome P450 reductase-null mice reveal a second microsomal reductase for squalene monooxygenase (2007), Arch. Biochem. Biophys., 461, 76-84.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information in hepatocytes deficent for NADPH-cytochrome P450 reductase, the second microsomal reductase retains about 40% of the full activity for conversion of squalene to 2,3(s)-oxidosqualene with squalene monooxygenase, overview Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Mus musculus 5783
-
membrane
-
Mus musculus 16020
-
microsome
-
Mus musculus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
x * 64000 Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus squalene epoxidase interacts with NADPH-cytochrome P450 reductase and a second microsomal reductase for the conversion of squalene to 2,3(s)-oxidosqualene and to lanosterol in the cholesterol biosynthesis pathway, overview ?
-
?
squalene + AH2 + O2 Mus musculus
-
(S)-squalene-2,3-epoxide + A + H2O
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
hepatocyte primary Mus musculus
-
liver
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information squalene epoxidase interacts with NADPH-cytochrome P450 reductase and a second microsomal reductase for the conversion of squalene to 2,3(s)-oxidosqualene and to lanosterol in the cholesterol biosynthesis pathway, overview Mus musculus ?
-
?
squalene + AH2 + O2
-
Mus musculus (S)-squalene-2,3-epoxide + A + H2O
-
?

Subunits

Subunits Comment Organism
? x * 64000 Mus musculus

Cofactor

Cofactor Comment Organism Structure
FAD
-
Mus musculus