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Information on EC 1.13.11.62 - linoleate 10R-lipoxygenase
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1.13.11.62 linoleate 10R-lipoxygenaseIUBMB Comments
The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergillus spp.
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Word Map
- 1.13.11.62
- diol
-
linoleic
- fumigatus
-
dioxygenation
- hydroperoxide
-
8r-dioxygenase
- cyclooxygenase-1
-
antarafacial
- cys
-
8r-hydroperoxylinoleic
-
aspergilli
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
(10R)-dioxygenase, 10R-dioxygenase, 10R-DOX, PpoC, Psi-producing oxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10R-dioxygenase
10R-DOX
PpoC
Psi-producing oxygenase
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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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PATHWAY SOURCE
PATHWAYS
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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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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
-
-
?
palmitoleate + O2
8-hydroperoxy-9(Z)-hexadecenoic acid
-
low activity
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
moderate activity
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
moderate activity
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
the enzyme is involved in biosynthesis of oxylipins
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
best substrate
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
-
-
?
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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
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
the enzyme is involved in biosynthesis of oxylipins
-
-
?
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
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
purified recombinant enzyme, substrate palmitoleate, pH 8.0, 30°C
0.485
-
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
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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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). PPOC_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
1121
0
126460
Swiss-Prot
other Location (Reliability: 5)
A0A5K1K8Q8_9APHY
141
0
15999
TrEMBL
other Location (Reliability: 2)
A0A084G0A2_PSEDA
964
0
106915
TrEMBL
other Location (Reliability: 4)
A0A5K1K7Q2_9APHY
392
0
42608
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F8BQ22_CERFI
1110
0
123534
TrEMBL
other Location (Reliability: 2)
A0A5K1JZB9_9APHY
220
0
23967
TrEMBL
other Location (Reliability: 5)
A0A084FUV8_PSEDA
1137
0
127002
TrEMBL
other Location (Reliability: 1)
Q4W941_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
1136
0
129161
TrEMBL
-
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PROTEIN VARIANTS
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
-
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
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garscha, U.; Oliw, E.H.
Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis oF (10R)-dioxygenase with epoxyalcohol synthase activity
J. Biol. Chem.
284
13755-13765
2009
Aspergillus fumigatus (Q4WY82), Aspergillus fumigatus
brenda
Jernerén, F.; Garscha, U.; Hoffmann, I.; Hamberg, M.; Oliw, E.H.
Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
Aspergillus clavatus (Q4W941), Aspergillus clavatus
brenda
Han, J.E.; Seo, M.J.; Shin, K.C.; Oh, D.K.
Production of 10R-hydroxy unsaturated fatty acids from hempseed oil hydrolyzate by recombinant Escherichia coli cells expressing PpoC from Aspergillus nidulans
Appl. Microbiol. Biotechnol.
100
7933-7944
2016
Aspergillus nidulans, Aspergillus nidulans ATCC 10074
brenda
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