1.14.14.17: squalene monooxygenase
This is an abbreviated version!
For detailed information about squalene monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.17
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1.14.14.17
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cholesterol
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sterol
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terbinafine
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ergosterol
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trichophyton
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mevalonate
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lanosterol
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allylamine
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2,3-oxidosqualene
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hmg-coa
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itraconazole
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mentagrophytes
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rubrum
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oxidosqualene
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terbinafine-resistant
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tellurium
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tinea
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naftifine
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interdigitale
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antimycotic
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bloch
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griseofulvin
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dammarenediol
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dermatophytoses
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cycloartenol
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beta-amyrin
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medicine
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corporis
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drug development
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nutrition
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biotechnology
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pharmacology
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cholesterogenic
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synthesis
- 1.14.14.17
- cholesterol
- sterol
- terbinafine
- ergosterol
- trichophyton
- mevalonate
- lanosterol
- allylamine
- 2,3-oxidosqualene
- hmg-coa
- itraconazole
- mentagrophytes
- rubrum
- oxidosqualene
-
terbinafine-resistant
- tellurium
- tinea
- naftifine
- interdigitale
-
antimycotic
-
bloch
-
griseofulvin
-
dammarenediol
-
dermatophytoses
- cycloartenol
- beta-amyrin
- medicine
-
corporis
- drug development
- nutrition
- biotechnology
- pharmacology
-
cholesterogenic
- synthesis
Reaction
Synonyms
CYP17, cytochrome P450 17alpha hydroxylase/17,20 lyase, EC 1.14.13.132, EC 1.14.99.7, Erg1, Erg1 protein, Erg1p, hydroxylase, squalene, oxygenase, squalene mono-, PgSQE1, PgSQE2, SE, SE1, SE3, SQE, SQE-I, SQE-II, sqe1, SQE3, SQLE, squalen expoxidase, squalene 2,3-epoxidase, squalene 2,3-oxidocyclase, squalene epoxidase, squalene epoxidase 1, squalene epoxidase 3, squalene hydroxylase, squalene mono-oxygenase, squalene oxydocyclase, squalene-2,3-epoxidase, squalene-2,3-epoxide cyclase, TkSQE1, TkSQE2, TkSQE3, TkSQE4
ECTree
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Cofactor
Cofactor on EC 1.14.14.17 - squalene monooxygenase
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FAD
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binding domain structure, the enzyme contains two highly conserved motifs 1 and 2, which flank the FAD cofactor and form part of the interface between cofactor and substrate binding domains in the structure modelling, overview
FAD
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sequence determination of the FAD-binding site with the dinucleotide-binding GXGXXG motif, and DG and GD motif
FAD
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dependent on, binds at a domain with a Rossmann fold, containing the 25GlyXGlyXXGly30 sequence
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FAD is not essential for activity, 76.2% activity in the absence of FAD
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additional information
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electron transfer partner NADPH-cytochrome P450 reductase
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additional information
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5-carba-5-deazaFAD cannot replace FAD as cofactor
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additional information
the enzyme sequence contains a Rossmann-dinucleotide binding fold and NAD(P)-binding site
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additional information
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the enzyme sequence contains a Rossmann-dinucleotide binding fold and NAD(P)-binding site
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