1.13.11.62: linoleate 10R-lipoxygenase
This is an abbreviated version!
For detailed information about linoleate 10R-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.62
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1.13.11.62
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diol
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linoleic
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fumigatus
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dioxygenation
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heme
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oxylipins
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8r-dioxygenase
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nidulans
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aspergilli
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epoxidation
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unsaturated
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hydroperoxide
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epoxy
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tyr
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heterolytic
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9-hydroperoxy
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allene
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inter
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thiolate
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oxysporum
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antarafacial
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fusarium
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sporulation
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endemic
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human-pathogenic
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flavus
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mycotoxin
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scurf
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tritici
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magnaporthe
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solani
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grey
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graminearum
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verticillioides
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cyclooxygenase-1
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oryzae
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homolytic
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zymoseptoria
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8r-hydroperoxylinoleic
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hyphal
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synthesis
- 1.13.11.62
- diol
-
linoleic
- fumigatus
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dioxygenation
- heme
- oxylipins
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8r-dioxygenase
- nidulans
-
aspergilli
-
epoxidation
- unsaturated
- hydroperoxide
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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
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homolytic
-
zymoseptoria
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8r-hydroperoxylinoleic
-
hyphal
- synthesis
Reaction
Synonyms
(10R)-dioxygenase, 10R-dioxygenase, 10R-dioxygenase-epoxy alcohol synthase, 10R-DOX, 10R-DOX-EAS, PpoC, Psi-producing oxygenase
ECTree
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Engineering
Engineering on EC 1.13.11.62 - linoleate 10R-lipoxygenase
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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
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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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