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Information on EC 1.13.11.62 - linoleate 10R-lipoxygenase
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EC Tree
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
- heme
- oxylipins
-
8r-dioxygenase
- nidulans
-
aspergilli
-
epoxidation
- unsaturated
- hydroperoxide
-
epoxy
- tyr
-
heterolytic
-
9-hydroperoxy
-
allene
-
inter
-
thiolate
-
oxysporum
-
antarafacial
-
fusarium
-
sporulation
-
endemic
-
human-pathogenic
-
flavus
-
mycotoxin
-
scurf
-
tritici
-
magnaporthe
- solani
-
grey
-
graminearum
-
verticillioides
- cyclooxygenase-1
- oryzae
-
homolytic
-
zymoseptoria
-
8r-hydroperoxylinoleic
-
hyphal
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
10r-dox, 10r-dox-eas, 10r-dioxygenase, 10r-dioxygenase-epoxy alcohol synthase, (10r)-dioxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
10R-dioxygenase
10R-dioxygenase-epoxy alcohol synthase
10R-DOX
10R-DOX-EAS
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
-
-
?
alpha-linolenate + O2
10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate + 12(13)epoxy-10-hydroxy-(8E,15Z)-octadecadienoate
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
-
-
?
alpha-linolenate + O2
10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate + 12(13)epoxy-10-hydroxy-(8E,15Z)-octadecadienoate
-
-
-
?
alpha-linolenate + O2
10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate + 12(13)epoxy-10-hydroxy-(8E,15Z)-octadecadienoate
-
-
-
?
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-hydroperoxy-8,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
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-hydroperoxy-8,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
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)
A0A5K1JZB9_9APHY
220
0
23967
TrEMBL
other Location (Reliability: 5)
A0A5K1K7Q2_9APHY
392
0
42608
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0F8BQ22_CERFI
1110
0
123534
TrEMBL
other Location (Reliability: 2)
A0A084G0A2_PSEDA
964
0
106915
TrEMBL
other Location (Reliability: 4)
A0A084FUV8_PSEDA
1137
0
127002
TrEMBL
other Location (Reliability: 1)
A0A8J8WLI3_9EURO
1117
0
125704
TrEMBL
other Location (Reliability: 3)
F9FAJ9_FUSOF
Fusarium oxysporum (strain Fo5176)
1283
0
144297
TrEMBL
other Location (Reliability: 2)
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
Jernern, 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
Oliw, E.H.
Linoleate diol synthase related enzymes of the human pathogens Histoplasma capsulatum and Blastomyces dermatitidis
Arch. Biochem. Biophys.
696
108669
2020
Blastomyces dermatitidis
brenda
Oliw, E.; Hamberg, M.
An allene oxide and 12-oxophytodienoic acid are key intermediates in jasmonic acid biosynthesis by Fusarium oxysporum
J. Lipid Res.
58
1670-1680
2017
Fusarium oxysporum (F9FAJ9), Fusarium oxysporum, Fusarium oxysporum Fo5176 (F9FAJ9)
brenda
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