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Enzyme Nomenclature
Information on EC 1.11.2.3 - plant seed peroxygenase
Word Map on EC 1.11.2.3
- 1.11.2.3
-
arachidonic
-
epoxyeicosatrienoic
- renal
- epoxide
-
cyclooxygenase
- artery
-
lipoxygenase
-
vasodilation
-
eicosanoids
- indomethacin
-
hyperpolarizing
-
cyp2j2
-
dihydroxyeicosatrienoic
- miconazole
- 20-hete
-
20-hydroxyeicosatetraenoic
-
endothelium-derived
-
cyp-derived
-
endothelium-dependent
-
dhets
-
oleosins
-
edhfs
-
vasodilatory
-
vasoconstrictor
-
nordihydroguaiaretic
-
arteriolar
-
ms-ppoh
-
preglomerular
-
p450-derived
-
regioisomeric
- sulfaphenazole
-
iberiotoxin
-
cross-recognition
-
hydroxyeicosatetraenoic
-
17-odya
-
omega-hydroxylase
-
epoxygenation
-
edhf-mediated
-
preconstricted
-
14,15-epoxyeicosa-5z-enoic
- 1-aminobenzotriazole
-
p450-dependent
-
large-conductance
-
5,6-epoxyeicosatrienoic
- skf525a
- cyp2c11
-
17-octadecynoic
-
11,12-epoxyeicosatrienoic
-
eicosatetraynoic
-
cyp-dependent
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.11.2.3
-
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RECOMMENDED NAME
GeneOntology No.
plant seed peroxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
R1H + R2OOH = R1OH + R2OH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epoxidation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
substrate:hydroperoxide oxidoreductase (RH-hydroxylating or epoxidising)
A heme protein with calcium binding motif (caleosin-type). Enzymes of this type include membrane-bound proteins found in seeds of different plants. They catalyse the direct transfer of one oxygen atom from an organic hydroperoxide, which is reduced into its corresponding alcohol to a substrate which will be oxidized. Reactions catalysed include hydroxylation, epoxidation and sulfoxidation. Preferred substrate and co-substrate are unsaturated fatty acids and fatty acid hydroperoxides, respectively. Plant seed peroxygenase is involved in the synthesis of cutin.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
inactivation of peroxygenase results in a dramatic decrease of cuticular epoxide content accompanied by a reduced thickness of the cuticle
malfunction
-
inactivation of peroxygenase results in a dramatic decrease of cuticular epoxide content accompanied by a reduced thickness of the cuticle
malfunction
-
inactivation of peroxygenase results in a dramatic decrease of cuticular epoxide content accompanied by a reduced thickness of the cuticle
physiological function
-
peroxygenase is able to catalyze in vitro the epoxidation step required for the biosynthesis of C18 cutin monomers
physiological function
-
peroxygenase is able to catalyze in vitro the epoxidation step required for the biosynthesis of C18 cutin monomers
physiological function
-
peroxygenase is able to catalyze in vitro the epoxidation step required for the biosynthesis of C18 cutin monomers
physiological function
-
the membrane-bound isoform of caleosin plays a putative role as a peroxygenase involved in oxylipin metabolism during biotic and abiotic stress responses in Arabidopsis. Clo-3 is involved in the generation of oxidised fatty acids in stress-related signalling pathways involving both ABA and salicylic acid. Clo-3 is part of an oxylipin pathway induced by multiple stresses and may also generate fatty acid derived anti-fungal compounds for plant defence
physiological function
at the seed germination stage, a loss-of-function mutant is hypersensitive to abscisic acid, salt and mannitol stresses, whereas isoform CLO4-overexpressing lines are more hyposensitive to those stresses than the wild type. In adult stage, loss-of-function mutant and overexpressing plants show enhanced and decreased drought tolerance, respectively. Following exposure to exogenous abscisic acid, the expression of key abscisic acid-dependent regulatory genes, such as ABF3 and ABF4, is up-regulated in the loss-of-function mutant, while it is down-regulated in overexpressing lines
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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
(+)-(R)-limonene + H2O2
(R)-limonene trans-1,2-epoxide
-
-
97% of products
-
?
(-)-(S)-limonene + H2O2
(S)-limonene cis-1,2-epoxide
-
-
88% of products
-
?
(10E,12Z,9S)-9-hydroperoxy-octadec-10,12-dienoate + H2O2
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O
(10E,12Z,9S)-9-hydroxy-octadec-10,12-dienoate + H2O2
(10E,12R,13S,9S)-12,13-epoxy-9-hydroxy-octadec-10-enoate + H2O
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O2
(10E,12R,13S,9S)-12,13-epoxy-9-hydroxy-octadec-10-enoate + H2O
-
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + tert-butyl hydroperoxide
(12Z,15Z)-9,10-epoxyoctadeca-12,15-dienoic aicd + (9Z,12Z)-15,16-epoxy-9,12-octadecadienoic acid + ?
-
-
-
-
?
10-cis-heptadecenoic acid + cumene hydroperoxide
10,11-epoxyheptadecanoic acid + ?
94% of the activity with oleic acid
-
-
?
10-cis-pentadecenoic acid + cumene hydroperoxide
10,11-epoxypentadecanoic acid + ?
98% of the activity with oleic acid
-
-
?
2 linolenic acid + 3 tert-butyl hydroperoxide
(12Z,15Z)-9-epoxyoctadec-12,15-dienoic acid + (12Z)-9,15-diepoxyoctadec-12-enoic acid + 3 tert-butanol
-
-
-
-
?
2-methylhept-1-ene + tert-butyl hydroperoxide
2-methyl-2-pentyloxirane + ?
-
-
-
-
?
9-cis-hexadecenoic acid + cumene hydroperoxide
9,10-epoxy hexadecanoic acid + ?
89% of the activity with oleic acid
-
-
?
cis-2-heptene + tert-butyl hydroperoxide
2-butyl-3-methyl-cis-oxirane + ?
-
-
93.9% yield
-
?
cis-3-heptene + tert-butyl hydroperoxide
2-ethyl-3-propyl-cis-oxirane + ?
-
-
72.7% yield
-
?
cyclohexene + tert-butyl hydroperoxide
7-oxabicyclo-[4.1.0]-heptane + ?
-
-
70.5% yield
-
?
gamma-terpinene + H2O2
p-cymene
-
-
in this reaction, hydroperoxide serves as hydrogen acceptor rather than an oxygen donor
-
?
linoleate + tert-butyl hydroperoxide
(9Z)-12,13-epoxyoctadec-9-enoate + (12Z)-9,10-epoxyoctadec-12-enoate + 9,10-12,13-diepoxy-octadecanoate + ?
-
-
23.4% yield, 25.4% yield and 46.7% yield, respectively
-
?
linoleate methyl ester + tert-butyl hydroperoxide
methyl 12,13-epoxy-9(Z)-octadecenoate + methyl 9,10-epoxy-12(Z)-octadecenoate + methyl 9,10-12,13-diepoxyoctadecanoate + ?
-
-
17.6% yield, 21.9% yield and 49.5% yield, respectively
-
?
linoleic acid + H2O2
15,16-epoxy-9,12-octadecadienoic acid + H2O
-
-
25% yield
-
?
linoleic acid + tert-butyl hydroperoxide
9,10-epoxy-octadecanoic acid + tert-butanol
-
-
-
-
?
linolenic acid + cumene hydroperoxide
linolenic acid 9,10-15,16-diepoxide + ?
74% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
major product, (R),(S)-epoxide enantiomers
-
?
methyl (13Z)-docos-13-enoate + tert-butyl hydroperoxide
methyl behenate 13,14-epoxide + H2O
-
-
26.9% yield
-
?
N-iso-butyl-(9Z,12Z,15Z)-octadecatrienamide + tert-butyl hydroperoxide
N-iso-butyl-9,10-15,16-diepoxy-(12Z)-octadecenamide + ?
-
-
-
-
?
oleate + tert-butyl hydroperoxide
methyl 9,10-epoxyoctadecanoate + ?
-
-
99.8% yield
-
?
oleate methyl ester + tert-butyl hydroperoxide
methyl 9,10-epoxyoctadecanoate + ?
-
-
93.9% yield
-
?
oleic acid + fatty acid hydroperoxide
cis-9,10-epoxystearic acid + ?
-
-
-
-
?
ricinoleate + tert-butyl hydroperoxide
9,10-epoxy-12-hydroxyoctadecanoate + ?
-
-
73.6% yield
-
?
trans-10,cis-12-linoleic acid + H2O2
12,13-epoxy-10-octadecenoic acid
-
-
epoxidation occurs only at cis-double bond
-
-
trans-2-heptene + tert-butyl hydroperoxide
2-butyl-3-methyl-trans-oxirane + ?
-
-
26.6% yield
-
?
(10E,12Z,9S)-9-hydroperoxy-octadec-10,12-dienoate + H2O2
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroperoxy-octadec-10,12-dienoate + H2O2
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroperoxy-octadec-10,12-dienoate + H2O2
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroperoxy-octadec-10,12-dienoate + H2O2
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroperoxy-octadec-10,12-dienoate + H2O2
(10E,12Z,9S)-9-hydroxyoctadec-10,12-dienoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroxy-octadec-10,12-dienoate + H2O2
(10E,12R,13S,9S)-12,13-epoxy-9-hydroxy-octadec-10-enoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroxy-octadec-10,12-dienoate + H2O2
(10E,12R,13S,9S)-12,13-epoxy-9-hydroxy-octadec-10-enoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroxy-octadec-10,12-dienoate + H2O2
(10E,12R,13S,9S)-12,13-epoxy-9-hydroxy-octadec-10-enoate + H2O
-
-
-
-
?
(10E,12Z,9S)-9-hydroxy-octadec-10,12-dienoate + H2O2
(10E,12R,13S,9S)-12,13-epoxy-9-hydroxy-octadec-10-enoate + H2O
-
-
-
-
?
linoleate + H2O2
(12Z,9R,10S)-9,10-epoxyoctadec-12-enoate + H2O
-
-
-
-
?
linoleic acid + cumene hydroperoxide
?
-
64% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
-
?
linoleic acid + cumene hydroperoxide
?
47% of the activity with oleic acid
-
-
?
oleic acid + cumene hydroperoxide
cis-9,10-epoxystearic acid + ?
-
-
-
-
?
linolenate + tert-butyl hydroperoxide
additional information
-
-
-
0.6% monoepoxy product and 91.6% diepoxy product
-
?
methyl linolenate + tert-butyl hydroperoxide
additional information
-
-
-
14.3% monoepoxy product and 78.3% diepoxy product
-
?
additional information
?
-
enzyme is an efficient fatty acid epoxygenase, catalyzing the oxidation of cis double bonds of unsaturated fatty acids. The C-12,13 double bond of these unsaturated fatty acids is the least favoured. Isoform PXG4 catalyzes exclusively the formation of (R),(S)-epoxide enantiomers, which is the absolute stereochemistry of the epoxides found in planta. Poor substrate: oleic acid methyl ester
-
-
-
additional information
?
-
-
the enzyme does not oxidize diacylglycerol and triacylglycerol
-
-
-
additional information
?
-
isoform PXG1 catalyzes the strictly hydroperoxide-dependent epoxidation of unsaturated fatty acids. It prefers hydroperoxy-trienoic acids over hydroperoxydienoic acids as oxygen donors to oxidize a wide range of unsaturated fatty acids with cis double bonds. Phospholipids and acyl-CoA are not effective substrates and it will only use free fatty acid or fatty acid methyl esters as substrates. Both hydroperoxy-dienoic and hydroperoxy-trienoic acids are effectively utilized as oxygen donors, with hydroperoxy-trienoic acids being more efficiently reduced
-
-
-
additional information
?
-
-
peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule
-
-
-
additional information
?
-
-
thiobenzamide and thioacetamide are no substrates
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + tert-butyl hydroperoxide
(12Z,15Z)-9,10-epoxyoctadeca-12,15-dienoic aicd + (9Z,12Z)-15,16-epoxy-9,12-octadecadienoic acid + ?
-
-
-
-
?
2 linolenic acid + 3 tert-butyl hydroperoxide
(12Z,15Z)-9-epoxyoctadec-12,15-dienoic acid + (12Z)-9,15-diepoxyoctadec-12-enoic acid + 3 tert-butanol
-
-
-
-
?
linoleic acid + tert-butyl hydroperoxide
9,10-epoxy-octadecanoic acid + tert-butanol
-
-
-
-
?
linolenic acid + cumene hydroperoxide
linolenic acid 9,10-15,16-diepoxide + ?
Q9CAB7
74% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
major product, (R),(S)-epoxide enantiomers
-
?
oleic acid + fatty acid hydroperoxide
cis-9,10-epoxystearic acid + ?
-
-
-
-
?
linoleic acid + cumene hydroperoxide
?
Q9CAB7
-
64% conversion, physiological linoleic and linolenic acids are the preferred substrates for isoform PXG4
-
?
oleic acid + cumene hydroperoxide
cis-9,10-epoxystearic acid + ?
-
-
-
-
?
additional information
?
-
Q9CAB7
enzyme is an efficient fatty acid epoxygenase, catalyzing the oxidation of cis double bonds of unsaturated fatty acids. The C-12,13 double bond of these unsaturated fatty acids is the least favoured. Isoform PXG4 catalyzes exclusively the formation of (R),(S)-epoxide enantiomers, which is the absolute stereochemistry of the epoxides found in planta. Poor substrate: oleic acid methyl ester
-
-
-
additional information
?
-
-
the enzyme does not oxidize diacylglycerol and triacylglycerol
-
-
-
additional information
?
-
-
peroxygenase exists in nature as a complex with a carotenoid-binding macromolecule
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
the purified enzyme preparation contains 3.2 nmol of protoheme/mg of protein
heme
contains a protoheme of type b, with 0.6 nmol of heme per mg protein
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
the enzyme contains a Ca2+ binding motif, calcium is crucial for its peroxygenase activity
Ca2+
-
the enzyme contains a Ca2+ binding motif, calcium is crucial for peroxygenase activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
the sulfoxidation of thiobenzamide, catalyzed by isoform PXG1, is completely abolished in the presence of 1 mM 2-mercaptoethanol (competitive inhibitor)
terbufos
-
a suicide substrate for plant peroxygenases, and at a concentration of 3 mM, it effectively inactivates the activity of isoform PXG1
terbufos
-
48% residual activity at 0.01 mM and 27% residual activity at 0.02 mM
additional information
-
paraoxon has no effect on oleic acid epoxidase activity
-
additional information
-
paraoxon ethyl has no effect on oleic acid epoxidase activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
linoleic acid hydroperoxide
-
partially purified enzyme, at pH 7.2 and 25°C
0.07
indole
-
partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C
0.08
indole
-
partially purified enzyme, using linoleic acid hydroperoxide as cosubstrate, at pH 7.2 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
O,O-dimethyl O-(4-nitrophenyl)phosphorothioate
Avena sativa
-
in 0.1 M KH2PO4, at pH 7.0 and 26°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.1
-
partially purified enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate
7.2
-
membrane-bound enzyme, using 0.2 mM linoleic acid hydroperoxide as cosubstrate; partially purified enzyme, using 1.0 mM H2O2 as cosubstrate
9.5
-
for both (2E)-4-hydroxy-2-hexenal and (2E)-4-hydroxy-2-nonenal formation the optimal pH is 9.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
dominantly expressed in vascular bundles in most organs as well as in the guard cells
dominantly expressed in vascular bundles in most organs as well as in the guard cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 25000, seed-specific isoform Clo-1, SDS-PAGE; x * 27000, microsomal isoform Clo-3, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
sumoylation
-
isoform PXG1 possesses a high sumoylation potentiality at the position Lys-196
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21, determined at -173°C as TRIS-complex, 2.8 A resolution, 88.2% overall completeness
Soja hispida
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme immobilized on various polyaniline-based polymers retains 80% of its activity for 15 weeks. Immobilized enzyme shows a greatly improved tolerance to different organic solvents
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetonitrile
-
soluble enzyme loses about 90% of its activity in 70% acetonitrile, the immobilized enzyme loses about 30% of its activity
Glycerol
-
20% (v/v) glycerol remarkably stabilizes the enzyme. The enzyme extracted with cholate or deoxycholate is very stable in the presence of glycerol
Triton X-100
-
the solubilized peroxygenase is unstable especially in the presence of Triton X-100
Tween
-
the solubilized peroxygenase is unstable especially in the presence of Tween 80
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Trisacryl 300 gel filtration and CM-Sepharose column chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is down-regulated following exposure to exogenous abscisic acid and salt stress
isoform Clo-3 is highly upregulated following exposure to abiotic stresses, such as salt and drought or treatment with salicylic acid or 2,6-dichloroisonicotinic acid, and to biotic stress such as Leptosphaeria maculans infection
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H138V
-
the mutant possess only 4% of the heme content wild type isoform PXG1
H70V
-
the heme content of the mutant is barely measurable (less than 1%) as compared to the wild type isoform PXG1
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LINKS TO OTHER DATABASES (specific for EC-Number 1.11.2.3)
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