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Literature summary extracted from

  • Lee, H.K.; Zheng, Y.F.; Xiao, X.Y.; Bai, M.; Sakakibara, J.; Ono, T.; Prestwich, G.D.
    Photoaffinity labeling identifies the substrate-binding site of mammalian squalene epoxidase (2004), Biochem. Biophys. Res. Commun., 315, 1-9.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.17 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.17 D407F site-directed mutagenesis, mutant shows 8% of wild-type activity Rattus norvegicus
1.14.14.17 K399F site-directed mutagenesis, mutant shows 28% of wild-type activity Rattus norvegicus
1.14.14.17 K399F/R400F/D407F site-directed mutagenesis, triple mutant shows 10% of wild-type activity Rattus norvegicus
1.14.14.17 K399P/R400P/D407P site-directed mutagenesis, triple mutant shows 10% of wild-type activity Rattus norvegicus
1.14.14.17 K399W/R400W/D407W site-directed mutagenesis, inactive mutant Rattus norvegicus
1.14.14.17 additional information construction of a truncated enzyme mutant Rattus norvegicus
1.14.14.17 R400F site-directed mutagenesis, mutant shows 24% of wild-type activity Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.17 26-hydroxysqualene competitive Rattus norvegicus
1.14.14.17 NB-598 squalenoid noncompetitive allylamine inhibitor Rattus norvegicus
1.14.14.17 trisnorsqualene alcohol squalenoid noncompetitive inhibitor, mechanism-based inactivator Rattus norvegicus
1.14.14.17 trisnorsqualene alcohol diazoester i.e. TNSA-Dza, competitive, able to photocovalently modify the native protein Rattus norvegicus
1.14.14.17 trisnorsqualene cyclopropylamine squalenoid noncompetitive inhibitor, mechanism-based inactivator Rattus norvegicus
1.14.14.17 trisnorsqualene hydroxylamine mechanism-based inactivator Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.17 50000
-
2 * 50000, recombinant truncated mutant enzyme, SDS-PAGE Rattus norvegicus
1.14.14.17 100000
-
recombinant truncated mutant enzyme Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.17 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.17 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.17 squalene + [reduced NADPH-hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O active site involves the key residues K399, R400, and D407 Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.17 additional information location of the substrate-binding site by binding studies using the photolabeling inhibitor trisnorsqualene alcohol diazoester, key residues are K399, R400, and D407 Rattus norvegicus ?
-
?
1.14.14.17 squalene + reduced acceptor + O2
-
Rattus norvegicus (S)-squalene-2,3-epoxide + acceptor + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.14.17 dimer 2 * 50000, recombinant truncated mutant enzyme, SDS-PAGE Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
1.14.14.17 SE
-
Rattus norvegicus
1.14.14.17 squalene epoxidase
-
Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.14.17 37
-
assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.17 7.4
-
assay at Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.14.17 additional information
-
additional information inhibition kinetics Rattus norvegicus
1.14.14.17 0.0184
-
trisnorsqualene alcohol diazoester recombinant truncated enzyme mutant, pH 7.4, 37°C Rattus norvegicus