Information on EC 1.3.1.70 - DELTA14-sterol reductase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.3.1.70
-
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RECOMMENDED NAME
GeneOntology No.
DELTA14-sterol reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
DELTA14-reduction in steroids
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cholesterol biosynthesis I
-
-
cholesterol biosynthesis II (via 24,25-dihydrolanosterol)
-
-
cholesterol biosynthesis III (via desmosterol)
-
-
plant sterol biosynthesis
-
-
zymosterol biosynthesis
-
-
cholesterol biosynthesis
-
-
Steroid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
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SYSTEMATIC NAME
IUBMB Comments
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol:NADP+ DELTA14-oxidoreductase
This enzyme acts on a range of steroids with a 14(15)-double bond.
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CAS REGISTRY NUMBER
COMMENTARY hide
69403-07-2
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene fk, enzyme FK, and bifunctinal enzyme DIM1/CBB1/DWF1
-
-
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
higher plants
-
-
Manually annotated by BRENDA team
New Zealand white rabbits
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
FgERG24A and FgERG24B are deleted in Fusarium graminearum. Compared to the wild-type strain HN9-1, FgERG24A and FgERG24B deletion mutants do not show recognizable phenotypic changes in mycelial growth on potato dextrose agar or in virulence on wheat heads. FgERG24B deletion mutants exhibit significantly increased sensitivity to amine fungicides, including tridemorph, fenpropidin and spiroxamine. FgERG24A deletion mutants do not show changed sensitivity to any amine tested. The resistance of the FgERG24B deletion mutant to amines is restored by genetic complementation of the mutant with wild-type FgERG24B
metabolism
-
an inverse upregulation of lanosterol 14alpha-demethylase, CYP51, and downregulation of 14-SR expression under luteinizing hormone/follicle stimulating hormone stimulation functions as the machinery for FF-MAS accumulation in preovulatory follicles prior to ovulation in the rabbit, overview
physiological function
-
FgERG24B controls the intrinsic resistance of Fusarium graminearum to amines
additional information
TM7SF2 gene expression is controlled by cell sterol levels through the SREBP-2, motifs of TM7SF2 promoter responsible for activation by SREBP-2 are the SRE motif, and both the inverted CCAAT-box and GC-box2, which are essential for full promoter activation by SREBP-2, overview. Binding of SREBP-2 to SRE produces approximately 26fold promoter activation, whereas mutation of the SRE motif causes a dramatic decrease of transactivation by SREBP-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol + NADPH
4,4-dimethyl-5alpha-cholesta-7-en-3beta-ol + NADP+
show the reaction diagram
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
show the reaction diagram
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
show the reaction diagram
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + NADPH + H+
4alpha-methylfecosterol + NADP+
show the reaction diagram
4alpha-methyl-8,14,24(28)-ergostatrien-3beta-ol + NADPH
4alpha-methyl-8,24(28)-ergostadien-3beta-ol + NADP+
show the reaction diagram
5alpha-cholesta-7,14-dien-3beta-ol + NADPH
5alpha-cholesta-7-en-3beta-ol + NADP+
show the reaction diagram
-
43% activity compared with 4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol
-
-
?
5alpha-cholesta-8,14-dien-3beta-ol + NADP+
5alpha-cholesta-8-en-3beta-ol + NADP+
show the reaction diagram
5alpha-cholesta-8,14-dien-3beta-ol + NADPH
5alpha-cholesta-8-en-3beta-ol + NADP+
show the reaction diagram
5alpha-ergosta-8,14,24(28)-trien-3beta-ol + NADPH
5alpha-ergosta-8,24(28)-dien-3beta-ol + NADP+
show the reaction diagram
cholesta-8,14-dien-3beta-ol + NADPH
cholesta-8-en-3beta-ol + NADP+
show the reaction diagram
ergosta-8,14-dien-3beta-ol + NADPH
ergosta-8-en-3beta-ol + NADP+
show the reaction diagram
-
DELTA8,14-sterol, ignosterol
-
-
?
follicular fluid meiosis-activating sterol + NADPH
testicular meiosis-activating sterol + NADP+
show the reaction diagram
-
-
-
-
?
isofucosterol + NADPH
sitosterol + NADP+
show the reaction diagram
additional information
?
-
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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
4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH
4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+
show the reaction diagram
4,4-dimethyl-5alpha-cholesta-8,14-dien-3beta-ol + NADPH
4,4-dimethyl-5alpha-cholesta-8-en-3beta-ol + NADP+
show the reaction diagram
-
presumably the natural substrate
-
-
?
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + NADPH + H+
4alpha-methylfecosterol + NADP+
show the reaction diagram
-
step in the biosynthesis of the brassicasterol phytohormones, catalyzed by enzyme FK
-
-
-
4alpha-methyl-8,14,24(28)-ergostatrien-3beta-ol + NADPH
4alpha-methyl-8,24(28)-ergostadien-3beta-ol + NADP+
show the reaction diagram
5alpha-cholesta-8,14-dien-3beta-ol + NADPH
5alpha-cholesta-8-en-3beta-ol + NADP+
show the reaction diagram
O76062, Q14739
the substrate accumulates in patients suffering autosomal recessive HEM/Greenberg skeletal dysplasia
-
-
?
follicular fluid meiosis-activating sterol + NADPH
testicular meiosis-activating sterol + NADP+
show the reaction diagram
-
-
-
-
?
isofucosterol + NADPH
sitosterol + NADP+
show the reaction diagram
-
step in the biosynthesis of the brassicasterol phytohormones, catalyzed by bifunctinal enzyme DIM1/CBB1/DWF1
-
-
-
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation by Mg2+ or Ca2+, 0.5-20 mM, but slight inhibition
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15-aza-24-methylene-D-homocholestadiene-3beta-ol
15-azasterol
2-amino-nonyl-6-methoxyl-tetralin muriate
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-
25-hydroxy-cholesterol
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IC50: 0.45 mM
3beta-(2-(diethylamino)ethoxy)androst-5-en-17-one
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U18666A, IC50: 0.004 mM
4-(3-[[1-(4-bromophenyl)piperidin-4-yl](methyl)amino]-1-methoxypropyl)benzonitrile
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using a genetic aproach in Saccharomyces cerevisiae it is shown that ERG24 is the target enzyme of compound 4-(3-[[1-(4-bromophenyl)piperidin-4-yl](methyl)amino]-1-methoxypropyl)benzonitrile
8-aza-4alpha,10-dimethyl-trans-decal-3beta-ol
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A25822B
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competitive inhibitor
amorolfine
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-
AY9944-A-7
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enzyme-specific inhibitor, leads to apoptosis in vivo at high concentrations in cumulus cells of oocytes
brefeldin
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inhibition of growth of mutant strains NJ25, NJ50, NJ51, and NJ55, not of wild-type strain and mutant NJ25, overview
cerulenin
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inhibition of growth of mutant strains NJ25, NJ50, NJ51, and NJ55, not of wild-type strain and mutant NJ25, overview
cholesterol
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enzyme suppressed by feeding 5% cholesterol, 70% decrease in enzyme activity
clotrimazole
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inhibition of growth of wild-type and mutant strains NJ25, NJ50, NJ51, and NJ55, overview
cyanide
cycloheximide
Detergents
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enzyme solubilization by detergents: inactivation
fenpropidin
fenpropimorph
fluconazole
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inhibition of growth of wild-type and mutant strain NJ25, only slightly of mutant strains NJ50, NJ51, and NJ55, overview
fluphenazine
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inhibition of growth of mutant strains NJ25, NJ50, NJ51, and NJ55, not of wild-type strain and mutant NJ25, overview
HgCl2
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3 mM: more than 99% inhibition, inhibition negligible in the presence of 10 mM glutathione
itraconazole
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inhibition of growth of wild-type and mutant strain NJ25, only slightly of mutant strains NJ50, NJ51, and NJ55, overview
ketoconazole
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inhibition of growth of wild-type and mutant strains NJ25, NJ50, NJ51, and NJ55, overview
miconazole
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IC50: 0.15 mM
N(1,5,9-trimethyldecyl)-4alpha,10-dimethyl-8-aza-trans-decal-3beta-ol
N-alkyl morpholine derivatives
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fungicides
N-alkyl-8-aza-4alpha,10-dimethyl-trans-decal-3beta-ol
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N-Benzyl-8-aza-4alpha,10-dimethyl-trans-decal-3beta-ol
N-dodecyl-8-aza-4alpha,10-dimethyl-trans-decal-3beta-ol
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N-ethylmaleimide
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5 mM: 53% inhibition, inhibition negligible in the presence of 10 mM glutathione
N-substituted 8-azadecalins
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potent inhibitors
N-[(3)-4-tert-butylphenyl-(2-methyl)propyl]-8-aza-4alpha,10-dimethyl-trans-decal-3beta-ol
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NADP+
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in the absence of NADPH-regenerating system, Ki: 0.45 mM; no inhibition by NAD+
Nystatin
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inhibition of growth of wild-type and mutant strain NJ25, not of mutants strains NJ50, NJ51, and NJ55, overview
O2
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28% inhibition
Phospholipase A2
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very high inhibition by very small concentrations, activity not restored by addition of phospholipids or any components presumed to be released from treated microsomes. Various concentration ranges of potential cofactors including FMN, FAD, AMP, ADP, ATP, coenzyme Q, Coenzyme A, and hemin, plus heat-treated microsomes, and lipid extracts of microsomes does not restore microsomal 14-reductase of phospholipase A2-treated microsomes
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spiroxamine
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sulfhydryl-binding agents
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-
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terbinafine
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inhibition of growth of mutant strains NJ25, NJ50, NJ51, and NJ55, not of wild-type strain and mutant NJ25, overview
trans-1,4-bis(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
tridemorph
Triparanol
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4-chloro-alpha-[4-[2-diethylaminoethoxy]phenyl]-alpha-(4-methylphenyl)benze-methanol, slight inhibition
Tris-HCl
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Tris-HCl buffer, 28% inhibition, not restored by addition of KCl at various concentrations
Triton X-100
-
-
Tween 80
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concentrations of Tween 80 higher than 1.5 g/l: inhibitory effect
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chelating agents
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slight activation
cholestyramine
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11fold induction and activation by feeding 5% cholestyramine plus 0.1% lovastatin, CL-diet. 2fold induction and activation by feeding 5% cholestyramine alone
-
EDTA
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slight activation
liposome
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activity of purified enzyme totally dependent on the presence of liposome and NADPH
-
lovastatin
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11fold induction and activation by feeding 5% cholestyramine plus 0.1% lovastatin, CL-diet. 4fold induction and activation by feeding 0.1% lovastatin alone
phosphatidylcholine
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liposomal phosphatidylcholine, egg yolk: 1.4fold activation
Phospholipids
-
partially purified enzyme: activation
additional information
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0294 - 0.0345
4,4-dimethyl-5alpha-cholesta-7,14-dien-3beta-ol
0.1
4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol
-
-
0.45
5alpha-cholesta-8,14-dien-3beta-ol
-
-
0.06
ergosta-8,14-dien-3beta-ol
-
ignosterol, Lineweaver-Burk plots
0.023 - 0.6
NADPH
additional information
additional information
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00003
15-azasterol
0.45
25-hydroxy-cholesterol
Rattus norvegicus
-
IC50: 0.45 mM
0.004
3beta-(2-(diethylamino)ethoxy)androst-5-en-17-one
Rattus norvegicus
-
U18666A, IC50: 0.004 mM
0.0018 - 0.003
fenpropidin
0.0008 - 0.0023
fenpropimorph
0.15
miconazole
Rattus norvegicus
-
IC50: 0.15 mM
0.0003 - 0.04
trans-1,4-bis(2-chlorobenzylaminomethyl)cyclohexane dihydrochloride
0.098
tridemorph
Saccharomyces cerevisiae
-
slight inhibitor, IC50: 0.098 mM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0555
-
partially purified enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at, aerobically
7.8
-
-
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 6.8
-
about 50% of maximum activity
6.5 - 9
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-
7
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DELTA8,14-streol DELTA14-reductase has relatively broad pH profile in the basic region with optimal pH at pH 7.8, activity decreases rapidly at pH below 7
7.8
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14-reductase has relatively broad pH profile in acidic region, activity drastically decreases with only moderate elevation of pH above 7.8
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LBR; TM7SF2 shows the highest mRNA expression
Manually annotated by BRENDA team
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highest expression of LBR
Manually annotated by BRENDA team
-
LBR
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
of an 18-weeks-old fetus with autosomal recessive HEM/Greenberg skeletal dysplasia showing enzyme-deficiency
Manually annotated by BRENDA team
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foetal and adult; in foetal heart the expression is much lower then in the adult heart, TM7SF2
Manually annotated by BRENDA team
-
foetal and adult, LBR; TM7SF2
Manually annotated by BRENDA team
-
peripheral blood leukocyte, LBR
Manually annotated by BRENDA team
-
foetal and adult, LBR
Manually annotated by BRENDA team
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LBR; TM7SF2
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
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during meiotic resumption of oocytes
Manually annotated by BRENDA team
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LBR; TM7SF2
Manually annotated by BRENDA team
-
foetal and adult, LBR; LBR
Manually annotated by BRENDA team
-
LBR; TM7SF2
Manually annotated by BRENDA team
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foetal and adult, LBR; in foetal thymus expression is much higher than in the adult thymus, TM7SF2
Manually annotated by BRENDA team
-
LBR; TM7SF2
Manually annotated by BRENDA team
-
LBR
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
inner nuclear membrane, LBR
Manually annotated by BRENDA team
additional information
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Methylomicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46600
x * 46600, mutant TM7SF2
46750
-
cloned cDNA, calculated from amino-acid sequence. The discrepancy between the apparent molecular mass of 38000 Da estimated by SDS-PAGE and the calculated molecular mass may be due to an aberrant electrophoretic migration
50610
-
amino acid analysis
70000
-
fast performance liquid chromatography
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 46600, mutant TM7SF2
dimer
-
2 * 38000, two equally-sized subunits, SDS-PAGE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
detergents such as Lubrol-WX, Emulgen 911, Triton X-100, Triton WR-1339, and their combinations with ionic detergents such as taurodeoxycholate, cholate, and Na+ salts destroy enzyme even at low concentration, 0.1-0.5%, w/v
-
enzyme in soluble form is very instable
-
enzyme very labile
stable against trypsin treatment
-
very labile membrane-bound enzyme, totally dependent on the presence of liposome and NADPH
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 1 week, stable
-
4°C, overnight, 30% activity lost
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial; Sephadex columns to de-salt enzyme preparation: 5fold activation
-
solubilization with combined octylglucoside and sodium taurodeoxycholate system and partial purification
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
14-SR, DNA and amino acid sequence determination and analysis, expression pattern, overview
-
a Neurospora crassa enzyme-deficient erg-3 mutant strain mat a and a yeast erg-4 mutant strain AP2 cannot be complemented by expression of 6 chimeric enzyme mutants variants constructed from the enzyme encoded by gene TM7SF2 and the Neurospora crassa gene erg-3 encoded enzyme
-
an enzyme-deficient erg-3 mutant strain mat a and a yeast erg-4 mutant strain AP2 cannot be complemented by expression of 6 chimeric enzyme mutants variants constructed from the enzyme encoded by erg-3 and the human gene TM7SF2 encoding the SR-1 protein
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cDNA expression in COS-7 cells; RT-PCR cloning; sterol DELTA14-reductase mRNA expression in bovine tisssues, high levels in liver and brain
-
DNA and amino acid sequence determination and analysis of 2 mutants, i.e. TM7SF2 and LBR, with autosomal recessive HEM/Greenberg skeletal dysplasia expressing a defective, truncated enzyme
expressed in Saccharomyces cerevisiae
-
expression of LBR in COS-1 cells; TM7SF2 expression in COS-1 cells
-
gene erg24, DNA and amino acid sequence determination, subcloning in Escherichia coli strain DH5alpha, complementation of the enzyme-deficient Saccharomyces cerevisiae erg24 mutant strain AP2
-
gene TM7SF2, promoter analysis, the promoter contains a 5'-ATTGG-3' sequence, an inverted CCAAT-box, 14 bp upstream the -73/-64 SRE-like motif, and is a region responsible for promoter regulation by sterols and by coexpressed SREBP-2, expression analysis, overview
TM7SF2 gene corresponds to DELTA14-SR, sterol DELTA14-reductase
-
wild-type ERG24 gene, wild-type C-14 reductase
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2-amino-nonyl-6-methoxyl-tetralin muriate increases mRNA levels of sterol metabolism genes such as ERG24
-
luteinizing hormone and follicle stimulating hormone both downregulates expression of 14-SR with the progression of antral follicular development
-
TM7SF2 gene expression is controlled by cell sterol levels through the SREBP-2, motifs of TM7SF2 promoter responsible for activation by SREBP-2 are the SRE motif, and both the inverted CCAAT-box and GC-box2, which are essential for full promoter activation by SREBP-2, overview. Binding of SREBP-2 to SRE produces approximately 26fold promoter activation
TM7SF2 gene expression is controlled by cell sterol levels through the SREBP-2, mutation of the SRE motif causes a dramatic decrease of transactivation by SREBP-2
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D207N
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
D227N
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
D276N
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
D289E
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
D289N
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
D293N
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
D394N
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
D462N
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
D463N
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
E22Q
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
E233D
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
E233Q
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
E475Q
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
G225C
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
H388A
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
H457A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
K229A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
K351A
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
K351R
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
K469A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
R212A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
R217A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
R235A
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
R235K
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
R345A
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
R355A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
R458A
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
R458K
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
R461A
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
R461K
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
T371A
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y124F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y273F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y317F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y391F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y445F
-
site-directed mutagenesis, mutant cannot complement enzyme-deficient erg-3 mutant strain mat a
Y447F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y470F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y477F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
Y490F
-
site-directed mutagenesis, mutant can complement enzyme-deficient erg-3 mutant strain mat a
additional information
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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target for important antifungal agents for use in the control of plant diseases
analysis
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partial purified enzyme suitable for reconstitution studies, reconstitution of isolated, soluble enzymes involved in cholesterol biosynthesis from lanosterol
pharmacology
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enzyme is a potential antifungal target site, development of antifungal compounds
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.70)
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)