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Literature summary for 1.14.14.17 extracted from

  • Laden, B.P.; Tang, Y.; Porter, T.D.
    Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase (2000), Arch. Biochem. Biophys., 374, 381-388.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of cDNA in Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Selenite recombinant enzyme Homo sapiens
selenium dioxide recombinant enzyme Homo sapiens
tellurite 17 mM, 50% non-competitive inhibition of the recombinant enzyme Homo sapiens
tellurium dioxide 37 mM, 50% inhibition of the recombinant enzyme Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000014
-
reduced NADPH-cytochrome P450 reductase recombinant enzyme, Km for electron transfer partner NADPH-cytochrone P 450 reductase Homo sapiens
0.3
-
FAD recombinant enzyme Homo sapiens
7.7
-
squalene recombinant enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-2,3-epoxy-2,3-dihydrosqualene + FAD + H2O
-
Homo sapiens squalene + FADH2 + O2
-
r
squalene + O2 + AH2
-
Homo sapiens 2,3 oxidosqualene + A + H2O
-
?
squalene + reduced NADPH-cytochrome P450 reductase + O2
-
Homo sapiens (3S)-2,3-epoxy-2,3-dihydrosqualene + oxidized NADPH-cytochrome P450 reductase + H2O
-
r

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0183
-
squalene
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD FAD is loosely bound Homo sapiens
additional information electron transfer partner NADPH-cytochrome P450 reductase Homo sapiens