1.14.14.17: squalene monooxygenase

This is an abbreviated version!
For detailed information about squalene monooxygenase, go to the full flat file.

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

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

                1.14.14.17 squalene monooxygenase

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Results	in table
15	Activating Compound
4611	AA Sequence
9	Application
1	CAS Registry Number
32	Cloned(Commentary)
41	Cofactor
2	Crystallization (Commentary)
167	Disease/ Diagnostics
14	Expression
22	General Information
2	General Stability
4	IC50 Value
154	Inhibitors
15	Ki Value [mM]
21	KM Value [mM]
27	Localization
1	Metals/Ions
16	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
154	Organism
7	Pathway
6	PDB ID
8	pH Optimum
7	pI Value
71	Protein Variants
15	Purification (Commentary)
5	Reaction
4	Reaction Type
81	Reference
2	Renatured (Commentary)
69	Source Tissue
8	Specific Activity [micromol/min/mg]
5	Storage Stability
71	Substrates and Products (Substrate)
18	Subunits
83	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
6	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.14.17 - squalene monooxygenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

analysis of the terbinafine-squalene epoxidase mode of interaction by docking studies followed by molecular dynamics simulations and quantum interaction energy calculations. In the energetically most likely orientation of terbinafine its interaction energy with the protein is ca. 120 kJ/mol. In the favorable position the terbinafine lipophilic moiety is located vertically inside the squalene epoxidase binding pocket with the tert-butyl group oriented toward its center, resulting in squalene epoxidase conformational changes and preventing the natural substrate from being able to bind to the enzyme's active site. Strongest interaction between terbinafine and squalene poxide stems from hydrogen bonding between hydrogen-bond donors, hydroxyl group of Tyr90 and amine nitrogen atom of terbinafine

Saccharomyces cerevisiae

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715725

homology model of enzyme based on p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens

Saccharomyces cerevisiae

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671379