Information on EC 1.13.11.61 - linolenate 9R-lipoxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.13.11.61
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RECOMMENDED NAME
GeneOntology No.
linolenate 9R-lipoxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-linolenate + O2 = (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
alpha-linolenate:oxygen (9R)-oxidoreductase
In cyanobacteria the enzyme is involved in oxylipin biosynthesis. The enzyme also converts linoleate to (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
Nostoc sp. PCC7120
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-linolenate + O2
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
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i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
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-
?
linoleate + O2
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
-
the enzyme is involved in oxylipin biosyntesis
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026
alpha-linolenate
-
pH 7.5, 22°C, wild-type enzyme
0.0044 - 0.0089
linoleate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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broad pH-optimum
7.3
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 70900, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of separate domains of NspLOX and the entire protein in Escherichia coli
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recombinant carboxy-terminal domain is purified after expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Nostoc sp. PCC7120
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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
Nostoc sp. PCC7120
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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
Nostoc sp. PCC7120
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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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