Information on EC 5.4.99.8 - Cycloartenol synthase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
5.4.99.8
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RECOMMENDED NAME
GeneOntology No.
Cycloartenol synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3S)-2,3-epoxy-2,3-dihydrosqualene = cycloartenol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
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intramolecular
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isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
7-dehydroporiferasterol biosynthesis
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avenacin biosynthesis, initial reactions
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Biosynthesis of secondary metabolites
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diploterol and cycloartenol biosynthesis
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ergosterol biosynthesis II
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mangrove triterpenoid biosynthesis
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Metabolic pathways
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plant sterol biosynthesis
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Steroid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(S)-2,3-Epoxysqualene mutase (cyclizing, cycloartenol-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9075-25-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
Ochromonas malhamensis
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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antisense inhibition of cycloartenol synthase results in decreased phytosterol levels and enhanced ginsenoside levels
metabolism
physiological function
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cycloartenol synthase is responsible for the synthesis of cycloartenol providing skeletons for phytosterols
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3S)-2,3-oxidosqualene
cycloartenol
show the reaction diagram
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?
(S)-2,3-Epoxysqualene
Cycloartenol
show the reaction diagram
(S)-2,3-oxidosqualene
cycloartenol
show the reaction diagram
1-trans-1'-Norsqualene-2,3-epoxide
31-Norcycloartenol
show the reaction diagram
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1-cis-1'-norsqualene-2,3-epoxide is not significantly cyclized
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oxidosqualene
cycloartenol
show the reaction diagram
additional information
?
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key enzyme in phytosterol biosynthesis
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-2,3-Epoxysqualene
Cycloartenol
show the reaction diagram
(S)-2,3-oxidosqualene
cycloartenol
show the reaction diagram
oxidosqualene
cycloartenol
show the reaction diagram
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sterol synthesis in plants
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?
additional information
?
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key enzyme in phytosterol biosynthesis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
Ochromonas malhamensis
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enzyme is inactive in absence of KCl, stimulation at concentrations up to 0.35 M, at higher levels slight fall of activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Aza-2,3-dihydro-squalene-N-oxide
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2-Aza-2,3-dihydrosqualene
2-hydroxyethyl jasmonate
downregulation of gene expression at 200 mM, diethydithiocarbamate depresses the down-regulation of CAS gene expression by 2-hydroxyethyl jasmonate
3beta-(2-Diethylaminoethoxy)androstenone
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8-Azadecalin
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Carbenium ion intermediate analogue inhibitors
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methyl jasmonate
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inhibits CaCYS transcription
Monocyclic 4-hydroxypiperidine
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N-Lauryl-N-dimethylamino-N-oxide
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N-[(1,5,9)-Trimethyl-decyl]-4alpha,10-dimethyl-8-aza-trans-decal-3beta-ol
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p-chloromercuribenzene sulfonic acid
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p-hydroxymercuribenzoate
Ochromonas malhamensis
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Sodium deoxycholate
Ochromonas malhamensis
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stimulates at low concentrations, optimal activation at 0.1%. Inhibition at levels greater than 0.5%
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Iminosqualene
Ochromonas malhamensis
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dithiothreitol
Ochromonas malhamensis
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stimulates
Sodium deoxycholate
Triton X-100
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the enzyme requires Triton X-100 or deoxycholate for maximal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 0.125
(S)-2,3-epoxysqualene
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00019
Ochromonas malhamensis
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
7 - 7.3
Ochromonas malhamensis
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
Ochromonas malhamensis
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30 min incubation
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.39
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81000
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calculated from nucleotide sequence
86300
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calculated from amino acid sequence
100000
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HPLC gel filtration
110000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Ochromonas malhamensis
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, cloning and expression in Escherichia coli strain D5alpha, functional expression of GST-tagged enzyme in Schizosaccharomyces pombe
expressed in Escherichia coli and in the yeast mutant GIL77
expressed in Saccharomyces cerevisiae mutant GIL77 cells
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expression in DH5-alpha Escherichia coli competent cells
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expression in Escherichia coli
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expression in Sacchaormyces cerevisiae
expression in Saccharomyces cerevisiae
expression in yeast
gene is present in single copy. Expression of enzyme in Saccharomyces cerevisiae
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mutants are expressed in Saccharomyces cerevisiae strain LHY4
sequence comparisons of lanosterol synthases and cycloartenol synthases from several organisms
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
plant derived and microbe derived elicitors altered WsOSCs expression pattern both at mRNA and protein level which corresponded with the change in the accumulation of three key withanolides namely withanolide A, withanone, and withaferin A, overview
the cycloartenol synthase gene in hairy root cultures elicited by 0.1 mM methyl jasmonate treatment decreases slightly
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H477N/I481V
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produces 99% lanosterol and 1% parkeol
H477Q/I481V
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produces 94% lanosterol and 6% parkeol
I481A
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production of lanosterol, cycloartenol, parkeol, acilleol A and camelliol C
I481F
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inactive
I481G
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production of lanosterol, cycloartenol, parkeol, acilleol A and camelliol C
I481L
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production of cycloartenol and parkeol
I481V
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produces 54% cycloartenol, 25% lanosterol, and 21% parkeol
Y410T
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produces 65% lanosterol, 2% parkeol, and 33% 9-beta-delta-7-lanosterol
Y410T/H477N/I481V
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produces 78% lanosterol and 22% 9-beta-delta-7-lanosterol
Y410T/H477Q/I481V
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produces 78% lanosterol and 22% 9-beta-delta-7-lanosterol
Y410T/I481V
Y532H
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mutated enzyme produces a mixture of parkeol, achilleol and lanosterol instead of cycloartenol
additional information
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mutation N478H/V482I in lanosterol synthase is a change of amino acids crucial for lanosterol specificity to the cycloartenol synthase type. Mutant produces 4% lanosterol, 83% parkeol, and 13% cycloartenol from substrate (S)-2,3-epoxysqualene, while wild-type lanosterol synthase produces only lanosterol