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Information on EC 1.14.18.10 - plant 4,4-dimethylsterol C-4alpha-methyl-monooxygenase
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EC Tree
1.14.18.10 plant 4,4-dimethylsterol C-4alpha-methyl-monooxygenaseIUBMB Comments
This plant enzyme catalyses a step in the biosynthesis of sterols. It acts on the 4alpha-methyl group of the 4,4-dimethylated intermediate 24-methylidenecycloartanol and catalyses three successive oxidations, turning it into a carboxyl group. The carboxylate is subsequently removed by EC 1.1.1.418, plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating), which also catalyses the epimerization of the remaining 4beta-methyl into the 4alpha position. Unlike the fungal/animal enzyme EC 1.14.18.9, 4alpha-methylsterol monooxygenase, this enzyme is not able to remove the methyl group from C-4-monomethylated substrates. That activity is performed in plants by a second enzyme, EC 1.14.18.11, plant 4alpha-monomethylsterol monooxygenase.
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Word Map
- 1.14.18.10
- ergosterol
-
demethylation
-
c4-methyl
- squalene
-
glabra2
-
acyl-coa-binding
-
histidine-rich
- cycloartenol
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
smo1-2, smo1-1, erg25a, 4alpha-methyl oxidase, sterol methyl oxidase, smo1-3, erg25b, 4,4-dimethylsterol-4alpha-methyl oxidase, sterol-4alpha-methyl oxidase, sterol-4alpha-methyl oxidase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4alpha-methyl oxidase
C4-sterol methyl oxidase
Erg25A
Erg25B
SMO
SMO1
SMO1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
24-methylidenecycloartanol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4alpha-(hydroxymethyl)-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferricytochrome b5 + H2O
(1a)
-
-
-
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+ = 3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
overall reaction
-
-
-
4alpha-(hydroxymethyl)-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 4alpha-formyl-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferricytochrome b5 + 2 H2O
(1b)
-
-
-
4alpha-formyl-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferrocytochrome b5 + O2 + 2 H+ = 3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-4alpha-carboxylate + 2 ferricytochrome b5 + H2O
(1c)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
24-methylidenecycloartanol,ferrocytochrome-b5:oxygen oxidoreductase (C-4alpha-methyl-hydroxylating)
This plant enzyme catalyses a step in the biosynthesis of sterols. It acts on the 4alpha-methyl group of the 4,4-dimethylated intermediate 24-methylidenecycloartanol and catalyses three successive oxidations, turning it into a carboxyl group. The carboxylate is subsequently removed by EC 1.1.1.418, plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating), which also catalyses the epimerization of the remaining 4beta-methyl into the 4alpha position. Unlike the fungal/animal enzyme EC 1.14.18.9, 4alpha-methylsterol monooxygenase, this enzyme is not able to remove the methyl group from C-4-monomethylated substrates. That activity is performed in plants by a second enzyme, EC 1.14.18.11, plant 4alpha-monomethylsterol monooxygenase.
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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
24(25)-dihydrocycloartenol + NAD(P)H + H+
?
-
30% activity compared to 24-methylidenecycloartanol
-
-
?
24-methylidenecycloartanol + 2 ferrocytochrome b5 + O2 + 2 H+
4alpha-(hydroxymethyl)-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferricytochrome B5 + H2O
-
-
-
-
?
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
24-methylidenecycloartanol + NAD(P)H + O2 + H+
4alpha-hydroxymethyl-4beta,14alpha-dimethyl-5alpha-ergosta-9beta,19-cyclo-24(241)-en-3beta-ol + NAD(P)+ + H2O
-
100% activity
-
-
?
24-methylidenecycloartanol + NADPH + O2 + H+
cycloeucalenol + NADP+ + H2O
-
overall reaction
-
-
?
24zeta-methylcycloartanol + NAD(P)H + H+
?
-
43% activity compared to 24-methylidenecycloartanol
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H+ + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferrocytochrome + H2O
1c
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + H2O
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + 3 H+ + 3 O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + 4 H2O
overall reaction
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + H+ + O2
4alpha-hydroxymethyl-4beta-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
1a
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
4-methyl fecosterol + 6 ferricytochrome b5 + 3 O2 + 6 H+
4,4-dimethyl fecosterol + 6 ferrocytochrome b5 + 4 H2O
4alpha-(hydroxymethyl)-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferrocytochrome b5 + O2 + 2 H+
4alpha-formyl-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-en-3beta-ol + 2 ferricytochrome b5 + H2O
-
-
-
-
?
4alpha-hydroxymethyl-4beta-methyl-5alpha-cholest-7-en-3beta-ol + reduced acceptor + H+ + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + acceptor + 2 H2O
1b
-
-
?
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H2O
cyclolaudenol + NAD(P)H + H+
?
-
56% activity compared to 24-methylidenecycloartanol
-
-
?
parkeol + 6 ferricytochrome b5 + 3 O2 + 6 H+
9(11)-dehydroergosterol + 6 ferrocytochrome b5 + 4 H2O
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
overall reaction
-
-
ir
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
overall reaction
-
-
?
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
-
overall reaction
-
-
?
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
-
overall reaction
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + H2O
step 3 of 3 of the overall reaction
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + H2O
step 3 of 3 of the overall reaction
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + H2O
step 3 of 3 of the overall reaction
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + H2O
-
step 3 of 3 of the overall reaction
-
-
?
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + a ferricytochrome + H2O
-
step 3 of 3 of the overall reaction
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
step 1 of 3 of the overall reaction
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
step 1 of 3 of the overall reaction
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
step 1 of 3 of the overall reaction
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
-
step 1 of 3 of the overall reaction
-
-
?
4,4-dimethyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferricytochrome + H2O
-
step 1 of 3 of the overall reaction
-
-
?
4-methyl fecosterol + 6 ferricytochrome b5 + 3 O2 + 6 H+
4,4-dimethyl fecosterol + 6 ferrocytochrome b5 + 4 H2O
-
i.e. 4,24-dimethyl-cholesta-8,24(28)-dien-3beta-ol
-
-
?
4-methyl fecosterol + 6 ferricytochrome b5 + 3 O2 + 6 H+
4,4-dimethyl fecosterol + 6 ferrocytochrome b5 + 4 H2O
-
i.e. 4,24-dimethyl-cholesta-8,24(28)-dien-3beta-ol
-
-
?
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H2O
step 2 of 3 of the overall reaction
-
-
?
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H2O
step 2 of 3 of the overall reaction
-
-
?
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H2O
step 2 of 3 of the overall reaction
-
-
?
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H2O
-
step 2 of 3 of the overall reaction
-
-
?
4beta-hydroxymethyl-4alpha-methyl-5alpha-cholest-7-en-3beta-ol + a ferrocytochrome + O2
3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carbaldehyde + a ferricytochrome + H2O
-
step 2 of 3 of the overall reaction
-
-
?
parkeol + 6 ferricytochrome b5 + 3 O2 + 6 H+
9(11)-dehydroergosterol + 6 ferrocytochrome b5 + 4 H2O
-
i.e. 4,4,14-trimethyl-cholesta-9(11),24-dien-3beta-ol
-
-
?
parkeol + 6 ferricytochrome b5 + 3 O2 + 6 H+
9(11)-dehydroergosterol + 6 ferrocytochrome b5 + 4 H2O
-
i.e. 4,4,14-trimethyl-cholesta-9(11),24-dien-3beta-ol
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
-
the enzyme is unable to oxidize 4,4-dimethylzymosterol
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO, sterol spectrum in wild-type and transgenic gene-silenced plants, accumulation of 4alpha-methyl-DELTA7-sterols, overview
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO, sterol spectrum in wild-type and transgenic gene-silenced plants, accumulation of 4alpha-methyl-DELTA7-sterols, overview
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
-
not catalyzed by P-450 but cytochrome b5 is suggested to be electron donor, NADPH and 24-methylenecycloartanol or 24-ethylidenelophenol
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
-
no activity with cyclobranol, cycloartenol, 24-methylenelanosterol, lanosterol, 24(25)-dihydrolanosterol, parkeol, 4,4-dimethyl-7,22-ergostadienol, beta-amyrine, 4alpha,14alpha,dimethyl-5alpha-cholesta-7-en-3beta-ol, obtusifoliol, 24zeta(241)-dihydroobtusifoliol, 29-norlanosterol, 24(25)-dihydro-29-norlanosterol, 4alpha-dimethyl-5alpha-cholestanol, 4alpha,14alpha,24zeta-trimethyl-5alpha-cholesta-9(11)-en-3beta-ol, and 4beta-24zeta(241)-dihydrocycloeucalenol
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
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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
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
24-methylidenecycloartanol + NADPH + O2 + H+
cycloeucalenol + NADP+ + H2O
-
overall reaction
-
-
?
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
overall reaction
-
-
ir
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
overall reaction
-
-
?
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
-
overall reaction
-
-
?
24-methylidenecycloartanol + 6 ferrocytochrome b5 + 3 O2 + 6 H+
3beta-hydroxy-4beta,14alpha-dimethyl-9beta,19-cyclo-5alpha-ergost-24(241)-ene-4alpha-carboxylate + 6 ferricytochrome b5 + 4 H2O
-
overall reaction
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO, sterol spectrum in wild-type and transgenic gene-silenced plants, accumulation of 4alpha-methyl-DELTA7-sterols, overview
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO, sterol spectrum in wild-type and transgenic gene-silenced plants, accumulation of 4alpha-methyl-DELTA7-sterols, overview
-
-
?
additional information
?
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
additional information
?
-
-
conversion of cycloartenol into functional phytosterol requires the removal of 2 methyl groups at C4 by the enzymic complex including the sterol 4alpha-methyl oxidase SMO
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IgG
-
polyclonal antibody raised against recombinant cytochrome b5, strongly inhibited of enzyme activity by low amounts of IgG, this results from IgG specific to cytochrome b5
-
additional information
-
not inhibited by stigmastan-3beta,5alpha,6alpha-triol
-
additional information
-
not inhibited by CO (saturated), LAB 170250F, and tetcyclacis
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
cytochrome c
Zea mays
-
using 24-methylenecycloartanol as substrate, at 30°C, pH not specified in the publication
0.01
cyanide
Zea mays
-
using 24-methylenecycloartanol as substrate, at 30°C, pH not specified in the publication
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme SMO1-1; 2 distinct enzyme families exist with 3 and 2 isozymes belonging to them, respectively
SwissProt
brenda
isozyme SMO1-2; 2 distinct enzyme families exist with 3 and 2 isozymes belonging to them, respectively
Swissprot
brenda
isozyme SMO1-3; 2 distinct enzyme families exist with 3 and 2 isozymes belonging to them, respectively
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
a erg25A deletion strain displays moderate susceptibility to hypoxia and the endoplasmic reticulum stress-inducing agent dithiothreitol, but is not required for virulence in murine or insect models of invasive aspergillosis
malfunction
-
a erg25A deletion strain displays moderate susceptibility to hypoxia and the endoplasmic reticulum stress-inducing agent dithiothreitol, but is not required for virulence in murine or insect models of invasive aspergillosis
-
physiological function
enzyme overexpression enhances total sterols and improves tolerance to osmotic/dehydration stress in transgenic tobacco plants
physiological function
-
isoform Erg25A is not required for virulence of Aspergillus fumigatus
physiological function
-
isoform Erg25A is not required for virulence of Aspergillus fumigatus
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SMO11_ARATH
298
4
34647
Swiss-Prot
other Location (Reliability: 2)
SMO12_ARATH
299
2
34989
Swiss-Prot
other Location (Reliability: 2)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
-
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
-
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
additional information
-
enzyme possesses 3 His-rich motifs common for membrane-bound non-heme iron oxygenases
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
virus-iduced gene silencing approach for reduction of enzyme expression, sterol analysis of transgenic plants
additional information
-
virus-iduced gene silencing approach for reduction of enzyme expression, sterol analysis of transgenic plants
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
DNA and amino acid sequence determination and analysis, expression in enzyme-lacking Saccharomyces cerevisiae strain erg25
DNA and amino acid sequence determination and analysis, in vitro transcription
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression significantly gets down-regulated (up to about 5fold) under salinity conditions with 400 mM NaCl. The enzyme expression is clearly down-regulated after 3 h treatment with 150 mg/ml chitosan or after 6 h treatment with 0.3 mM methyl jasmonate or after 1.5 h treatment with 1 mM salicylic acid or after 1.5 h treatment with 1 mM trans-cinnamic acid
transcript levels of the enzyme are consistently increased upon 0.01 mM abscisic acid or 0.1 mM gibberellic acid treatment and induced to more than 2fold relative to the control seedlings. Osmotic/dehydration stress with 400 mM mannitol markedly induces the transcript levels during 6-9 h of treatment and decreases then after
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rahier, A.; Smith, M.; Taton, M.
The role of cytochrome b5 in 4alpha-methyl-oxidation and C5(6) desaturation of plant sterol precursors
Biochem. Biophys. Res. Commun.
236
434-437
1997
Zea mays
brenda
Darnet, S.; Rahier, A.
Plant sterol biosynthesis: identification of two distinct families of sterol 4alpha-methyl oxidases
Biochem. J.
378
889-898
2004
Arabidopsis thaliana, Arabidopsis thaliana (F4JLZ6), Arabidopsis thaliana (Q1EC69), Arabidopsis thaliana (Q8L7W5), Zea mays, Nicotiana benthamiana (Q5J955), Nicotiana benthamiana, Nicotiana tabacum (Q6YAU5), Zea mays SMO1
brenda
Rahier, A.
Dissecting the sterol C-4 demethylation process in higher plants. from structures and genes to catalytic mechanism
Steroids
76
340-352
2011
Arabidopsis thaliana
brenda
Pascal, S.; Taton, M.; Rahier, A.
Oxidative C4-demethylation of 24-methylene cycloartanol by a cyanide-sensitive enzymatic system from higher plant microsomes
Biochem. Biophys. Res. Commun.
172
98-106
1990
Zea mays
brenda
Darnet, S.; Bard, M.; Rahier, A.
Functional identification of sterol-4alpha-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4alpha-methyl oxidation
FEBS Lett.
508
39-43
2001
Arabidopsis thaliana (Q8VWZ8), Arabidopsis thaliana (Q9ZW22), Arabidopsis thaliana
brenda
Zhang, J.; Li, X.; Lu, F.; Wang, S.; An, Y.; Su, X.; Li, X.; Ma, L.; Han, G.
De novo sequencing and transcriptome analysis reveal key genes regulating steroid metabolism in leaves, roots, adventitious roots and calli of Periploca sepium Bunge
Front. Plant Sci.
8
594
2017
Periploca sepium
brenda
Pascal, S.; Taton, M.; Rahier, A.
Plant sterol biosynthesis. Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation
J. Biol. Chem.
268
11639-11654
1993
Zea mays
brenda
Blosser, S.; Merriman, B.; Grahl, N.; Chung, D.; Cramer, R.
Two C4-sterol methyl oxidases (Erg25) catalyse ergosterol intermediate demethylation and impact environmental stress adaptation in Aspergillus fumigatus
Microbiology
160
2492-2506
2014
Aspergillus fumigatus, Aspergillus fumigatus CEA17
brenda
Singh, A.; Jindal, S.; Longchar, B.; Khan, F.; Gupta, V.
Overexpression of Artemisia annua sterol C-4 methyl oxidase gene, AaSMO1, enhances total sterols and improves tolerance to dehydration stress in tobacco
Plant Cell Tissue Organ Cult.
121
167-181
2015
Artemisia annua (A0A0A6YZ36)
-
brenda
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Release 2023.1 (January 2023)
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