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Enzyme Nomenclature
Information on EC 1.13.11.62 - linoleate 10R-lipoxygenase
for references in articles please use BRENDA:EC1.13.11.62
Word Map on EC 1.13.11.62
- 1.13.11.62
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diol
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linoleic
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hydroperoxide
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8r-dioxygenase
- fumigatus
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dioxygenation
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antarafacial
- cyclooxygenase-1
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8r-hydroperoxylinoleic
- cys
- fungus
- synthesis
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The expected taxonomic range for this enzyme is: Aspergillus
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EC NUMBER 
COMMENTARY 
1.13.11.62
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RECOMMENDED NAME
GeneOntology No.
linoleate 10R-lipoxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
linoleate:oxygen (10R)-oxidoreductase
The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergillus spp.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
the enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergilli
evolution
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Psi-producing oxygenases (Ppo enzymes) are classified as three enzyme types: PpoA (5,8-diol synthase), PpoB (suggested as 8,11-diol synthase), and PpoC (10R-dioxygenase)
evolution
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Psi-producing oxygenases (Ppo enzymes) are classified as three enzyme types: PpoA (5,8-diol synthase), PpoB (suggested as 8,11-diol synthase), and PpoC (10R-dioxygenase)
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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
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxy-8,12,15-octadecatrienoate
i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
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-
?
palmitoleate + O2
8-hydroperoxy-9(Z)-hexadecenoic acid
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low activity
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
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-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
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moderate activity
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-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
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-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
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moderate activity
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
the enzyme is involved in biosynthesis of oxylipins
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-10 with double bond migration
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergilli
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate, 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate and small amounts of 12S(13R)-epoxy-(10R)-hydroxy-(8E)-octadecenoic acid
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
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-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
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best substrate
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
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-
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-
?
additional information
?
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recombinant enzyme lacks hydroperoxide isomerase activity, but shows low epoxyalcohol synthase activity with biosynthesis of a novel oxylipin, 12S(13R)-epoxy-(10R)-hydroxy-18:1. The enzyme oxygenates 20:4n-6 (all-cis-5,8,11,14-eicosatetraenoic acid) i.e. by hydrogen abstraction at both C-13 and C-10 with formation of two nonconjugated and four cis-trans-conjugated hydroperoxyeicosatetraenoic acid
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-
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additional information
?
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recombinant enzyme lacks hydroperoxide isomerase activity, but shows low epoxyalcohol synthase activity with biosynthesis of a novel oxylipin, 12S(13R)-epoxy-(10R)-hydroxy-18:1. The enzyme oxygenates 20:4n-6 (all-cis-5,8,11,14-eicosatetraenoic acid) i.e. by hydrogen abstraction at both C-13 and C-10 with formation of two nonconjugated and four cis-trans-conjugated hydroperoxyeicosatetraenoic acid
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additional information
?
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the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
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-
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additional information
?
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assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
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-
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additional information
?
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the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
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-
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additional information
?
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assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
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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
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
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-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
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-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
Q4W941
the enzyme is involved in biosynthesis of oxylipins
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
Q4WY82
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergilli
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-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
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-
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?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
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-
-
-
?
additional information
?
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the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
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-
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additional information
?
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the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
linoleate
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.108
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purified recombinant enzyme, substrate palmitoleate, pH 8.0, 30°C
0.485
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purified recombinant enzyme, substrate alpha-linolenate, pH 8.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
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half-lives of recombinant PpoC in Escherichia coli cells at 30°C, 35°C, and 40°C are 530, 315, and 97 min, respectively, while those of purified recombinant enzyme are 41, 29, and 18 min, respectively. The half-lives of the recombinant enzyme in Escherichia coli cells are 12.9, 10.9, and 5.4fold higher at 30°C, 35°C, and 40°C, respectively, than those of the purified recombinant enzyme, indicating that thermal stability of recombinant PpoC in expressing cells is higher than that of the purified recombinant PpoC
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain ER2566 by nickel affinity chromatography and ultafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
functional recombinant expression of His-tagged enzyme in Escherichia coli strain ER2566
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L306A
the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate is slightly lowered
L306V
the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate is slightly lowered
L384A
the relative amount of (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate (8-HODE/(10-HODE + 8-HODE)) is 10.4% for the recombinant wild-type enzyme and 53.7% for the mutant enzyme. The L384A mutant changes the stereochemistry at C-8 and C-10. L384A forms the R and S enantiomers of 8-HODE and 10-HODE in a ratio of 3:2, whereas native and recombinant 10R-DOX form both products with 95% R configuration
L384F
increases the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate to 48% (the wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate and 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate)
L384M
increases the relative biosynthesis of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate compared to (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate with 3-4% units
L384V
the relative amount of (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate (8-HODE/(10-HODE + 8-HODE)) is 10.4% for the recombinant wild-type enzyme and 22.1% for the mutant enzyme
V388F
the wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate and 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate. The mutation increases the formation of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to 36%
V388L
the wild-type enzyme forms 90% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate and 10% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate. The mutation increases the formation of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to 16%
additional information
additional information
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under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC
additional information
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under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization
synthesis
-
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization
-
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