Information on EC 1.14.99.7 - squalene monooxygenase

for references in articles please use BRENDA:EC1.14.99.7
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.14.99.7
transferred to EC 1.14.13.132
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RECOMMENDED NAME
GeneOntology No.
squalene monooxygenase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
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LITERATURE
IMAGE
terbinafine
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noncompetitive inhibition, binding structure analysis, strongest interaction between terbinafine and enzyme stems from hydrogen bonding between hydrogen-bond donors, hydroxyl group of Tyr90 and amine nitrogen atom of terbinafine, mechanism of squalene epoxidase inhibition, overview. Inhibitor identification via docking studies followed by molecular dynamics simulations, based on PDB IDS 2QA1 and 1PBE templates, and quantum interaction energy calculations, overview
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
; weak expression of PgSQE2
Manually annotated by BRENDA team
; weak expression of PgSQE2
Manually annotated by BRENDA team
fine roots and root body
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PgSQE1 contains 4 putative transmembrane helices; PgSQE2 contains 3 putative transmembrane helices
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59100
x * 59100, about, sequence calculation
60200
x * 60200, about, sequence calculation
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59100, about, sequence calculation; x * 60200, about, sequence calculation
additional information
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the enzyme shows a two-domain structure with the FAD cofactor and the substrate binding domains
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene PgSQE1, DNA and amino acid sequence determination and analysis, phylogenetic analysis; gene PgSQE2, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
methyl jasmonate treatment suppresses expression of PgSQE2
squalene treatment coordinately upregulates the expression of PgSQE1, and methyl jasmonate treatment enhances the accumulation of PgSQE1 mRNA in roots. Silencing of PgSQE1 in RNAi roots strongly upregulates PgSQE2 and PNX, cycloartenol synthase, and results in enhanced phytosterol accumulation; squalene treatment coordinately upregulates the expression of PgSQE2. Silencing of PgSQE1 in RNAi roots strongly upregulates PgSQE2 and PNX, cycloartenol synthase, and results in enhanced phytosterol accumulation
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F402L
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the point mutation causes terbinafine resistance
F420L
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the point mutation causes terbinafine resistance
F430S
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the point mutation causes terbinafine resistance
L251F
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the point mutation causes terbinafine resistance
additional information
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
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squalene epoxidase is an attractive potential target for drugs used to inhibit the growth of pathogenic fungi or to lower cholesterol level in humans
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.7)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)