1.13.11.61: linolenate 9R-lipoxygenase
This is an abbreviated version!
For detailed information about linolenate 9R-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.61
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1.13.11.61
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linoleic
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diol
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ala
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dioxygenation
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lipoxygenases
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polyunsaturated
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nostoc
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cyanobacterial
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regio
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hydroperoxides
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aspergilli
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homolytic
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allene
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terreus
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stereochemistry
- 1.13.11.61
-
linoleic
- diol
- ala
-
dioxygenation
- lipoxygenases
-
polyunsaturated
- nostoc
-
cyanobacterial
-
regio
- hydroperoxides
-
aspergilli
-
homolytic
-
allene
- terreus
-
stereochemistry
Reaction
Synonyms
(9R)-LOX, 11R-LOX, 9R-lipoxygenase, 9R-LOX, ARA 11RLOX, arachidonate 11R-lipoxygenase, CspLOX2, LA 9RLOX, linoleate 11R-lipoxygenase, linoleate 9R-dioxygenase, lipoxygenase 2, NspLOX
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.11.61 - linolenate 9R-lipoxygenase
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A162G
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the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)
A162I
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the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)
A162V
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the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)
A162G
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the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)
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A162I
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the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)
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A162V
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the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)
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G401A
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site-directed mutagenesis, the mutaant shows increased formation of 11-hydroperoxyoctadeca-9,12-dienoate compared to the wild-type enzyme
I617L
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site-directed mutagenesis, the mutaant shows increased formation of 11-hydroperoxyoctadeca-9,12-dienoate compared to the wild-type enzyme
additional information
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Decreasing the channel size of a 9R-lipoxygenase (CspLOX1) can in turn induce formation of the bis-allylic 11R-hydroperoxide