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Information on EC 1.14.14.17 - squalene monooxygenase
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1.14.14.17 squalene monooxygenaseIUBMB Comments
A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7, lanosterol synthase, was formerly known as squalene oxidocyclase. The electron donor is EC 1.6.2.4, NADPH---hemoprotein reductase [5,7].
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Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
squalene epoxidase, squalene monooxygenase, erg1p, erg1 protein, pgsqe1, pgsqe2, tksqe1, squalene-2,3-epoxide cyclase, squalene mono-oxygenase, squalene epoxidase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.14.13.132
-
-
formerly
-
EC 1.14.99.7
-
-
formerly
-
Erg1
Erg1p
hydroxylase, squalene
-
-
-
-
oxygenase, squalene mono-
-
-
-
-
SE
SQLE
squalene 2,3-oxidocyclase
-
-
-
-
squalene epoxidase
squalene hydroxylase
-
-
-
-
squalene mono-oxygenase
squalene oxydocyclase
-
-
-
-
squalene-2,3-epoxidase
-
-
-
-
squalene-2,3-epoxide cyclase
-
-
-
-
squalene epoxidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
squalene + [reduced NADPH-hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
squalene + [reduced NADPH-hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
squalene + [reduced NADPH-hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
proposed mechanism
-
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
-
squalene + [reduced NADPH-hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
cytochrome P450 17alpha hydroxylase/17,20 lyase CYP17 also catalyzes the reaction of squalene epoxidase
-
squalene + [reduced NADPH-hemoprotein reductase] + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
aromatic amino acid residues located at the substrate-binding domain of the active-site, e.g. Ph223 and Tyr473, control the stereochemical course of the enzyme reaction, mechanism of regio- and stereo-specific epoxidation of squalene to (3S)2,3-oxidosqualene, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epoxidation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
squalene,NADPH-hemoprotein:oxygen oxidoreductase (2,3-epoxidizing
A flavoprotein (FAD). This enzyme, together with EC 5.4.99.7, lanosterol synthase, was formerly known as squalene oxidocyclase. The electron donor is EC 1.6.2.4, NADPH---hemoprotein reductase [5,7].
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CAS REGISTRY NUMBER
COMMENTARY
9029-62-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3S)-2,3-epoxy-2,3-dihydrosqualene + 1-carba-1-deaza-FAD + H2O
squalene + 1-carba-1-deaza-FADH2 + O2
-
-
-
-
r
(3S)-squalene-2,3-epoxide + AH2 + O2
(3S,22S)-2,3-22,23-dioxidosqualene + A + H2O
-
the wild-type enzyme also catalyzes conversion of (3S)2,3-oxidosqualene to (3S,22S)-2,3-22,23-dioxidosqualene
-
-
?
1,1-bisnorsqualene + NADPH + O2
1,1-bisnor-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
-
?
1-methylsqualene + NADPH + O2
1-methyl-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
1-norsqualene + NADPH + O2
1-norsqualene-2,3-epoxide + NADP+ + H2O
-
-
-
?
10,11,14,15-tetrahydrosqualene + NADPH + O2
10,11,14,15-tetrahydro-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
10,11-dihydrosqualene + NADPH + O2
10,11-dihydro-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
2,3-oxidosqualene + NADPH + O2
2,3,22,23-dioxidosqualene + NADP+ + H2O
-
N-terminal truncated recombinant enzyme
-
?
6,7,18,19-tetrahydrosqualene + NADPH + O2
6,7,18,19-tetrahydro-(S)-squalene-2,3-epoxide
-
-
-
?
squalene + reduced cytochrome P450 + H+ + O2
(3S)-squalene-2,3-epoxide + cytochrome P450 + H2O
absolutely stereo- and regiospecific reaction, co-reaction with NADPH-cytochrome P450 reductase
-
-
?
squalene + reduced cytochrome P450 + O2
(S)-squalene-2,3-epoxide + cytochrome P450 + H2O
first step in the cyclic chloesterol biosynthesis
-
-
?
squalene + reduced NADPH-cytochrome P450 reductase + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + oxidized NADPH-cytochrome P450 reductase + H2O
-
-
-
-
r
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
(3S)-2,3-epoxy-2,3-dihydrosqualene + FAD + H2O
squalene + FADH2 + O2
-
-
-
-
r
squalene + AH2 + O2
(3S)-squalene-2,3-epoxide + A + H2O
-
rate-limiting step in chloesterol biosynthesis
-
-
?
squalene + AH2 + O2
(3S)-squalene-2,3-epoxide + A + H2O
-
aromatic amino acid residues located at the substrate-binding domain of the active-site, e.g. Ph223 and Tyr473, control the stereochemical course of the enzyme reaction, mechanism of regio- and stereo-specific epoxidation of squalene to (3S)2,3-oxidosqualene, overview
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
production of the precursor for all known angiosperm cyclic triterpenoids, which include membrane sterols, brassinosteroid phytohormones, and non-steroidal triterpenoids, overview
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
oxidosqualene or dioxidosqualene appears to be the branching point for primary metabolism and secondary metabolites in basidiomycetes
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
rate-limiting enzyme in the triterpene saponins biosynthetic pathway, overview
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
-
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
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, substrate binding domain structure, overview
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
the enzyme is involved in ergosterol biosynthesis
-
-
?
squalene + electron donor + O2
(S)-squalene-2,3-epoxide + oxidized electron donor + H2O
-
-
-
-
?
squalene + electron donor + O2
(S)-squalene-2,3-epoxide + oxidized electron donor + H2O
-
first oxygenase and last nonsterol reaction of sterol biosynthesis
-
?
squalene + electron donor + O2
(S)-squalene-2,3-epoxide + oxidized electron donor + H2O
-
may be rate-limiting step in cholesterol biosynthesis in non-cholesterogenic tissues
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
NADH is preferred
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
NADH is preferred
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
-
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
NADPH is preferred
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
specific for NADPH
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
NADPH is preferred
-
?
squalene + NAD(P)H + O2
(S)-squalene-2,3-epoxide + NADP+ + H2O
-
NADPH is slightly preferred
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
-
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
epoxidation of squalene is the first step in cholesterol biosynthesis
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
-
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
epoxidation of squalene is the first step in cholesterol biosynthesis
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
-
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
epoxidation of squalene is the first step in cholesterol biosynthesis
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
-
the enzyme affects morphogenesis and drug susceptibilities
-
-
?
additional information
?
-
-
the enzyme activity is associated with cytochrome P450 17alpha hydroxylase/17,20 lyase CYP17 in cholesterol biosynthesis in Leydig cells
-
-
?
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
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
squalene + AH2 + O2
(3S)-squalene-2,3-epoxide + A + H2O
-
rate-limiting step in chloesterol biosynthesis
-
-
?
squalene + reduced cytochrome P450 + O2
(S)-squalene-2,3-epoxide + cytochrome P450 + H2O
first step in the cyclic chloesterol biosynthesis
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
production of the precursor for all known angiosperm cyclic triterpenoids, which include membrane sterols, brassinosteroid phytohormones, and non-steroidal triterpenoids, overview
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
oxidosqualene or dioxidosqualene appears to be the branching point for primary metabolism and secondary metabolites in basidiomycetes
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
rate-limiting enzyme in the triterpene saponins biosynthetic pathway, overview
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
-
-
-
?
squalene + AH2 + O2
(S)-squalene-2,3-epoxide + A + H2O
-
the enzyme is involved in ergosterol biosynthesis
-
-
?
squalene + electron donor + O2
(S)-squalene-2,3-epoxide + oxidized electron donor + H2O
-
first oxygenase and last nonsterol reaction of sterol biosynthesis
-
?
squalene + electron donor + O2
(S)-squalene-2,3-epoxide + oxidized electron donor + H2O
-
may be rate-limiting step in cholesterol biosynthesis in non-cholesterogenic tissues
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
epoxidation of squalene is the first step in cholesterol biosynthesis
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
epoxidation of squalene is the first step in cholesterol biosynthesis
-
-
?
squalene + reduced acceptor + O2
(S)-squalene-2,3-epoxide + acceptor + H2O
-
epoxidation of squalene is the first step in cholesterol biosynthesis
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
squalene + [reduced NADPH-hemoprotein reductase] + O2
(3S)-2,3-epoxy-2,3-dihydrosqualene + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
-
Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
-
-
?
additional information
?
-
-
the enzyme affects morphogenesis and drug susceptibilities
-
-
?
additional information
?
-
-
the enzyme activity is associated with cytochrome P450 17alpha hydroxylase/17,20 lyase CYP17 in cholesterol biosynthesis in Leydig cells
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
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
-
sequence determination of the FAD-binding site with the dinucleotide-binding GXGXXG motif, and DG and GD motif
FAD
-
dependent on, binds at a domain with a Rossmann fold, containing the 25GlyXGlyXXGly30 sequence
additional information
-
FAD is not essential for activity, 76.2% activity in the absence of FAD
-
additional information
-
electron transfer partner NADPH-cytochrome P450 reductase
-
additional information
-
5-carba-5-deazaFAD cannot replace FAD as cofactor
-
additional information
the enzyme sequence contains a Rossmann-dinucleotide binding fold and NAD(P)-binding site
-
additional information
-
the enzyme sequence contains a Rossmann-dinucleotide binding fold and NAD(P)-binding site
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-N-ethyl-N-(6,6-dimethyl-2-hepten-4-ynyl)-3-[2-methyl-2-(3-thienylmethoxy)propyloxy]benzylamine hydrochloride
-
trivial name FR194738, 0.0000098 mM, 50% inhibition of enzyme activity in HepG2 cell homogenate
1-[3-(2,3-dichlorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(2,4-dichlorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(2,5-dichlorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(2,6-dichlorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(3,4-dichlorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(3,5-dichlorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
strong, selective inhibition
1-[3-(3,5-difluorophenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(3-chloro-5-methoxyphenyl)-prop-2-ynyl]-3-methylpiperidine hydrochloride
-
-
1-[3-(3-methylphenyl)-prop-2-ynyl]