Information on EC 1.13.11.62 - linoleate 10R-lipoxygenase

for references in articles please use BRENDA:EC1.13.11.62
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The expected taxonomic range for this enzyme is: Aspergillus

EC NUMBER
COMMENTARY hide
1.13.11.62
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RECOMMENDED NAME
GeneOntology No.
linoleate 10R-lipoxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Linoleic acid metabolism
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
the enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergilli
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
(8E,10R,12Z,15Z)-10-hydroperoxy-8,12,15-octadecatrienoate
show the reaction diagram
i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
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-
?
alpha-linolenate + O2
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
show the reaction diagram
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
show the reaction diagram
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
show the reaction diagram
oleate + O2
8-hydroperoxy-9(Z)-octadecenoic acid
show the reaction diagram
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low activity
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?
palmitoleate + O2
8-hydroperoxy-9(Z)-hexadecenoic acid
show the reaction diagram
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low activity
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-
?
additional information
?
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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
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
show the reaction diagram
linoleate + O2
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
show the reaction diagram
linoleate + O2
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
show the reaction diagram
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
linoleate
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.065
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purified recombinant enzyme, substrate oleate, pH 8.0, 30C
0.108
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purified recombinant enzyme, substrate palmitoleate, pH 8.0, 30C
0.485
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purified recombinant enzyme, substrate alpha-linolenate, pH 8.0, 30C
0.761
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purified recombinant enzyme, substrate linoleate, pH 8.0, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
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over 70% of maximal activity within this range
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
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half-lives of recombinant PpoC in Escherichia coli cells at 30C, 35C, and 40C 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 30C, 35C, and 40C, 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
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
expression in SF21 cells
functional recombinant expression of His-tagged enzyme in Escherichia coli strain ER2566
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis