Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.58
-
RECOMMENDED NAME
GeneOntology No.
linoleate 9S-lipoxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
9-lipoxygenase and 9-allene oxide synthase pathway
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9-lipoxygenase and 9-hydroperoxide lyase pathway
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divinyl ether biosynthesis I
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Linoleic acid metabolism
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SYSTEMATIC NAME
IUBMB Comments
linoleate:oxygen 9-oxidoreductase
Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and alpha-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C9 position with (S)-configuration. The enzyme plays a physiological role during the early stages of seedling growth. The enzyme from Arabidopsis thaliana shows comparable activity towards linoleate and linolenate [4]. EC 1.13.11.12 (linoleate 13S-lipoxygenase) catalyses a similar reaction at another position of these fatty acids.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected in Shangrila County, Yunnan Province, China, gene AgLOX1
UniProt
Manually annotated by BRENDA team
ssp. vulgaris
-
-
Manually annotated by BRENDA team
Nockwang
UniProt
Manually annotated by BRENDA team
Nockwang
UniProt
Manually annotated by BRENDA team
L. Osbeck
-
-
Manually annotated by BRENDA team
Traveller’s Joy
-
-
Manually annotated by BRENDA team
cv. Reba B50 (Allen X stoneville 2B)
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Sun Smile
-
-
Manually annotated by BRENDA team
cv. Sun Smile
-
-
Manually annotated by BRENDA team
Giant Cavendishii AAA
-
-
Manually annotated by BRENDA team
gene Nb-9-LOX
-
-
Manually annotated by BRENDA team
L. cv. Nipponbare
SwissProt
Manually annotated by BRENDA team
Mill.
SwissProt
Manually annotated by BRENDA team
Mill.
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9E,11Z,14Z)-icosa-9,11,14-trienoic acid + O2
(9S,11Z,14Z)-9-hydroperoxyicosa-11,14-dienoic acid
show the reaction diagram
-
good substrate
-
-
?
AA/Lyso-PA + O2
15-HPETE/lyso-PA + 13-HPETE/lyso-PA + 15-HPETE/lyso-PA + 11-HPETE/lyso-PA + 5-HPETE/lyso-PA
show the reaction diagram
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-
36%, 22%, 21% and 13% yield, respectively
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?
alpha-linolenate
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
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(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate is the main product
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?
alpha-linolenate + O2
(10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
alpha-linolenate + O2
?
show the reaction diagram
comparable oxygenase activity with either linoleic acid or linolenic acid
no product determined
-
?
arachidonate + O2
?
show the reaction diagram
arachidonic acid + O2
5-HPETE + 7-HPETE + 9-HPETE
show the reaction diagram
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-
22%, 25% and 29% yield, respectively
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?
gamma-linolenate + O2
(6Z,9S,10E,12Z)-9-hydroperoxy-6,10,12-octadecatrienoate
show the reaction diagram
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72% (6Z,9S,10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoate, with racemic 6-, 10-, and 13-gamma-hydroperoxy-(10E,12Z,15Z)-octadecatrienoates as secondary products
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?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
additional information
?
-
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
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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contains Fe2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hydroperoxide
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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
9E,11Z,14Z-20:3omega6
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at pH 7.5 and 22°C
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0.0203
arachidonate
pH 6.5, 25°C
0.0039 - 0.15
linoleate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6
9E,11Z,14Z-20:3omega6
Homo sapiens
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at pH 7.5 and 22°C
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1.3
arachidonate
Capsicum annuum
D3TTH9
pH 6.5, 25°C
8.7 - 390
linoleate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.062
arachidonate
Capsicum annuum
D3TTH9
pH 6.5, 25°C
619
0.076
linoleate
Capsicum annuum
D3TTH9
pH 6.5, 25°C
808
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
pH 5.0: about 50% of maximal activity, pH 8.5: about 70% of maximal activity
5 - 7
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pH 5.0: about 50% of maximal activity, pH 7: about 70% of maximal activity
5.3 - 6.5
pH 5.3: about 80% of maximal activity, pH 6.5: about 40% of maximal activity
8 - 9
pH 8: 30% of optimal activity, pH 9: about 15% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
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10°C: about 45% of maximal activity, 50°C: about 65% of maximal activity
15 - 30
15°C: about 90% of maximal activity, 30°C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 5.3
isoelectric focusing
5.52
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sequence calculation
5.61
calculated from sequence
5.94
gene AgLOX1 sequence calculation
6.66
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
Manually annotated by BRENDA team
shoot apical meristem
Manually annotated by BRENDA team
ZmLOX5 is strongly inducible in leaves and stems by wounding but not in roots
Manually annotated by BRENDA team
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves. along tuber formation, Lox1 class transcripts are detected at the stolon stage, and their steady state levels increases during the early stages of tuber development
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
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gel filtration
93200
density gradient centrifugation
98000
calculated from sequence
99100
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified by nickel affinity chromatography using a N-terminal (His)6-tag
recombinnat enzyme partially from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressing full-length CaLOX1 in Escherichia coli as a fusion protein with an N-terminal His tag. Overexpression of CaLOX1 in Arabidopsis (Arabidopsis thaliana) conferres enhanced resistance to Pseudomonas syringae pv tomato, Hyaloperonospora arabidopsidis, and Alternaria brassicicola
expression in Escherichia coli
expression in insect cells; expression in insect cells
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gene AgLOX1, cloned from chitosan-induced seedling, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
gene Nb-9-LOX, DNA and amino acid sequence determination and analysis, overexpression in Saccharomyces cerevisiae, quantitative realtime PCR exxpression analysis
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heterologously expressed in Escherichia coli
overexpression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of a maize 9-LOX gene, ZmLOX3, increases steadily and peaks at 7 days after inoculation with Meloidogyne incognita root-knot nematodes
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expression of CaLOX1 is induced 1 h after infection by the virulent strain Ds1, peaks at 20 h, and decreased thereafter. Expression of CaLOX1 is significantly increased by mock inoculation. The induction of CaLOX1 transcript in mock-inoculated or virulent Xcv inoculated leaves may be due, in part, to the wounding effect. Treatment with ethylene, SA, NaCl, and methyl viologen significantly induces CaLOX1 in pepper leaves
GhLOX1 is highly expressed in the cultivar Reba B50 during the interaction with the avirulent race 18 of Xanthomonas campestris pv malvacearum. Transcription positively responds to both hormones salicylic acid and jasmonic acid
lipoxygenase expression is induced very rapidly only in the salt-tolerant cells and in a transient manner. The induction is specific to salt stress and does not occur with other osmotic-stress-inducing agents, such as polyethylene glycol or mannitol, or under hot or cold conditions, or in the presence of abscisic acid. The induction is eliminated by the antioxidants dithiothreitol and kaempferol
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the enzyme expression is highly induced by agroinfiltration of the plant leaves using a tobacco mosaic virus based vector system
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the enzyme is induced by low molecular weight chitosan, expression pattern, overview
transcripts of ZmLOX5 are increased in response to jasmonic acid and salicylic acid treatments. ZmLOX5 is transiently induced both locally and systemically by wounding
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A562G
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the product of the wild-type enzyme is 98.8% (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and 1.2% (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate. The product of mutant enzyme A562G is 68.9% (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and 31.1% (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate. Wild-type enzyme converts anandamide mainly to (11S)-hydroperoxyanandamide (99.4%). The mutant A562G forms (11S)-hydroperoxyanandamide and 15R-hydroperoxyanandamide in the ratio 3:2
A451G
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the mutant reacts well with arachidonic acid even in the absence of fatty acid hydroperoxides
A564G
the product of the wild-type enzyme is 99.1% (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and 0.9% (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate. The product of mutant enzyme A562G is 68.9% (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and 31.1% (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate. Wild-type enzyme converts anandamide mainly to (11S)-hydroperoxyanandamide (71%), plus 16% (5S)-hydroperoxyanandamide. The mutant enzyme A564G forms two additional prominent products, 15-hydroperoxyanandamide (34%) and 9-hydroperoxyanandamide (19%)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis