Information on EC 1.13.11.77 - oleate 10S-lipoxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.77
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RECOMMENDED NAME
GeneOntology No.
oleate 10S-lipoxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-linolenate + O2 = (8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
show the reaction diagram
(3)
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linoleate + O2 = (8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
show the reaction diagram
(2)
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oleate + O2 = (8E,10S)-10-hydroperoxyoctadeca-8-enoate
show the reaction diagram
(1)
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SYSTEMATIC NAME
IUBMB Comments
oleate:oxygen (10S)-oxidoreductase
Binds Fe2+. The enzyme isolated from the bacterium Pseudomonas sp. 42A2 has similar activity with all the three Delta9 fatty acids. cf. EC 1.13.11.62, linoleate 10R-lipoxygenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
(8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
show the reaction diagram
arachidonate + O2
?
show the reaction diagram
cis-12-octadecenoate + O2
?
show the reaction diagram
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8.9% activity compared to linoleate
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?
linoleate + O2
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
show the reaction diagram
oleate + O2
(8E,10S)-10-hydroperoxyoctadeca-8-enoate
show the reaction diagram
petroselenoate + O2
?
show the reaction diagram
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26.4% activity compared to linoleate
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?
triolein + O2
?
show the reaction diagram
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0.4% activity compared to linoleate
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?
vaccenic acid + O2
?
show the reaction diagram
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
linoleate + O2
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
show the reaction diagram
oleate + O2
(8E,10S)-10-hydroperoxyoctadeca-8-enoate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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the enzyme contains 0.55 mol of Fe2+ per mol of protein
Mg2+
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the presence of 1 mM Mg2+ increases enzyme activity 1.5fold
Mn2+
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the enzyme contains 25 mmol Mn2+ per mol of protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ba2+
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complete inhibition at 1 mM
EDTA
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99% inhibition at 5 mM
Fe3+
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complete inhibition at 1 mM
Mg2+
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concentrations of Mg2+ higher than 1.25 mM inhibit activity strongly (90% of activity lost at 1.75 mM)
oleate
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at concentrations of oleate higher than 2.1 mM, the enzyme activity is inhibited by excess of substrate
Zn2+
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complete inhibition at 1 mM
additional information
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not inhibited by 5 mM KCN
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.73
alpha-linolenate
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in 0.2 M sodium borate buffer, pH 9.0, at 30°C
0.66
linoleate
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in 0.2 M sodium borate buffer, pH 9.0, at 30°C
0.74
oleate
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in 0.2 M sodium borate buffer, pH 9.0, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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1 * 45000, SDS-PAGE
50000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 70
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44% of activity still remains at 55°C. The enzyme is stable up to 45 °C, but sharply decreases after 50°C. Activity is completely lost at 70°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 week, no loss of activity (thawing and freezing decreases enzyme activity by 30%)
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Q Sepharose column chromatography and Macro-Prep SE 100/40 gel filtration
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