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Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase
for references in articles please use BRENDA:EC1.13.11.58
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EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.11 With incorporation of two atoms of oxygen
1.13.11.58 linoleate 9S-lipoxygenase
IUBMB Comments
Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-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 . EC 1.13.11.12 (linoleate 13S-lipoxygenase) catalyses a similar reaction at another position of these fatty acids.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.13.11.58
-
linoleic
- oxylipins
-
9-loxs
- lipoxygenases
-
9s-hydroperoxide
-
13-lipoxygenase
-
divinyl
-
colneleic
-
trihydroxy
-
alpha-ketols
- epoxyalcohols
- 12r-lox
-
9s-hydroperoxy-10e,12z-octadecadienoic
- synthesis
showSynonyms
9-lipoxygenase, zmlox3, r9-lox1, zmlox5, calox1, atlox1, epidermal lipoxygenase-3, ghlox1, linoleate 9s-lipoxygenase, nb-9-lox, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
9-lipoxygenase
9-LOX
CaLOX1
linoleate 9-lipoxygenase
linoleate 9S-lipoxygenase
LOX
LOX1
LOX1.3
LOX12
LOX2
LOX3
LOX4
LOX5
LOX6
r9-LOX1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
9-lipoxygenase and 9-allene oxide synthase pathway, 9-lipoxygenase and 9-hydroperoxide lyase pathway, alpha-linolenate metabolites biosynthesis, divinyl ether biosynthesis I, linoleate metabolites biosynthesis, vernolate biosynthesis III
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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Substrates: good substrate
Products: -
Products: -
?
12-hydroperoxy-cis,trans,cis-9,13,15-octadecatrienoic acid + O2
12,13-epoxy-14-hydroxy-cis,cis-9,15-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
?
9-hydroperoxy-cis,trans,cis-6,10,12-octadecatrienoic acid + O2
9,10-epoxy-11-hydroxy-cis,cis-6,12-octadecadienoic acid
9-hydroperoxy-trans,cis-10,12-octadecadienoic acid + O2
9,10-epoxy-11-hydroxy-cis-12-octadecenoic acid
AA/Lyso-PA + O2
15-HPETE/lyso-PA + 13-HPETE/lyso-PA + 15-HPETE/lyso-PA + 11-HPETE/lyso-PA + 5-HPETE/lyso-PA
-
Substrates: -
Products: 36%, 22%, 21% and 13% yield, respectively
Products: 36%, 22%, 21% and 13% yield, respectively
?
alpha-linolenate
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Substrates: -
Products: (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate is the main product
Products: (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate is the main product
?
alpha-linolenate + O2
?
Substrates: comparable oxygenase activity with either linoleic acid or linolenic acid
Products: no product determined
Products: no product determined
?
arachidonic acid + O2
5-HPETE + 7-HPETE + 9-HPETE
-
Substrates: -
Products: 22%, 25% and 29% yield, respectively
Products: 22%, 25% and 29% yield, respectively
?
gamma-linolenate + O2
(6Z,9S,10E,12Z)-9-hydroperoxy-6,10,12-octadecatrienoate
Substrates: -
Products: 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
Products: 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
?
gamma-linolenic acid + O2
9 9-hydroperoxy-cis,trans,cis-6,10,12-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleic acid + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
linolenic acid + O2
9-hydroperoxy-6,10,12-octadecatrienoate
-
Substrates: -
Products: -
Products: -
?
linolenic acid + O2
9-hydroperoxy-trans,cis-10,12-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
?
9-hydroperoxy-cis,trans,cis-6,10,12-octadecatrienoic acid + O2
9,10-epoxy-11-hydroxy-cis,cis-6,12-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
?
9-hydroperoxy-cis,trans,cis-6,10,12-octadecatrienoic acid + O2
9,10-epoxy-11-hydroxy-cis,cis-6,12-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
?
9-hydroperoxy-trans,cis-10,12-octadecadienoic acid + O2
9,10-epoxy-11-hydroxy-cis-12-octadecenoic acid
-
Substrates: -
Products: -
Products: -
?
9-hydroperoxy-trans,cis-10,12-octadecadienoic acid + O2
9,10-epoxy-11-hydroxy-cis-12-octadecenoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenate + O2
(10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: -
Products: the R/S stereoconfiguration of the product is not determined
Products: the R/S stereoconfiguration of the product is not determined
?
alpha-linolenate + O2
(10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Substrates: -
Products: 96% (10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate and 2.1% (9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
Products: 96% (10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate and 2.1% (9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
?
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Substrates: comparable oxygenase activity with either linoleic acid or linolenic acid
Products: the enzyme forms exclusively (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Products: the enzyme forms exclusively (9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
?
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Substrates: -
Products: 12-, 13-, and 16-hydroperoxy-(10E,12Z,15Z)-octadecatrienoates are minor byproducts
Products: 12-, 13-, and 16-hydroperoxy-(10E,12Z,15Z)-octadecatrienoates are minor byproducts
?
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
Substrates: -
Products: -
Products: -
?
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
Substrates: comparable oxygenase activity with either linoleic acid or linolenic acid
Products: more than 96% of the substrate is converted to the the 9-positional hydroperoxide
Products: more than 96% of the substrate is converted to the the 9-positional hydroperoxide
?
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
Substrates: -
Products: -
Products: -
?
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenic acid + O2
12-hydroperoxy-cis,trans,cis-9,13,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
alpha-linolenic acid + O2
12-hydroperoxy-cis,trans,cis-9,13,15-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
gamma-linoleic acid + O2
9-hydroperoxy-cis,trans,cis-6,10,12-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
gamma-linoleic acid + O2
9-hydroperoxy-cis,trans,cis-6,10,12-octadecatrienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
Products: -
Products: -
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: -
Products: -
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: no formation of 13-hydroperoxy-(10E,12Z)-octadecadienoate. The R/S stereoconfiguration of the product is not determined
Products: no formation of 13-hydroperoxy-(10E,12Z)-octadecadienoate. The R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: -
Products: -
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: no formation of 13-hydroperoxy-(10E,12Z)-octadecadienoate. The R/S stereoconfiguration of the product is not determined
Products: no formation of 13-hydroperoxy-(10E,12Z)-octadecadienoate. The R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: the R/S stereoconfiguration of the product is not determined
Products: the R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is main product. The R/S stereoconfiguration of the product is not determined
Products: (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is main product. The R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is main product. The R/S stereoconfiguration of the product is not determined
Products: (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is main product. The R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: linoleate (abundant in membrane lipids of tubers) is preferred to linolenate as substrate
Products: the R/S stereoconfiguration of the product is not determined
Products: the R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: recombinant ZmLOX5 protein displays clear 9-LOX regiospecificity at both neutral and slightly alkaline pH
Products: the R/S stereoconfiguration of the product is not determined
Products: the R/S stereoconfiguration of the product is not determined
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: 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-9,11-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-9,11-octadecadienoate
Products: 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-9,11-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-9,11-octadecadienoate
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: comparable oxygenase activity with either linoleic acid or linolenic acid
Products: the enzyme forms exclusively (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Products: the enzyme forms exclusively (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: the main product (94%) is (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate, primarily S configuration
Products: the main product (94%) is (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate, primarily S configuration
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: regiospecificity of Nb-9-LOX, overview
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: low catalytic activity with complex substrates as compared to free linoleic acid. Residual relative activities lower than 1% with the substrates dilinolein, trilinolein, and 1-palmitoyl-2-linoleoyl-glycero-3-phosphocholine and with extracted lipids from malt confirm this supposition. However, LOX1 catalyzes HPODE formation from PamLinGroPCho with high regioselectivity (9-hydroperoxy-(10E,12Z)-octadecadienoate:13-hydroperoxy-(10E,12Z)-octadecadienoate) and high (9S)-hydroperoxy-(10E,12Z)-octadecadienoate stereoselectivity (S:R) (92:8)
Products: -
Products: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: -
Products: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: the enzyme specifically forms the 9-H(p)ODE isomer by 99.5%, 97.7% of which is in S-form
Products: -
Products: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: regiospecificity of Nb-9-LOX, overview
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: comparable oxygenase activity with either linoleic acid or linolenic acid
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: 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-9,11-octadecadienoate. The product of mutant enzyme A564G is 59.9% (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and 40.1% (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
Products: 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-9,11-octadecadienoate. The product of mutant enzyme A564G is 59.9% (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and 40.1% (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
Products: -
Products: -
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
Products: 98% (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate, almost exclusively S stereoconfiguration. (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate is a minor byproduct
Products: 98% (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate, almost exclusively S stereoconfiguration. (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate is a minor byproduct
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: 9-lipoxygenase does not utilize docosadienoic acid and catalyzes eicosadienoic acid dioxygenation 20fold slower than linoleic acid dioxygenation
Products: the enzyme specifically forms the S-stereoisomer
Products: the enzyme specifically forms the S-stereoisomer
?
linoleic acid + O2
9-hydroperoxy-trans,cis-10,12-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
?
linoleic acid + O2
9-hydroperoxy-trans,cis-10,12-octadecadienoic acid
-
Substrates: -
Products: -
Products: -
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additional information
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Substrates: from arachidonate the wild-type enzyme forms 47% 11-hydroxyeicosatetraenoic acid, 23% 5-hydroxyeicosatetraenoic acid, 11% 9-hydroxyeicosatetraenoic acid, 9% 12-hydroxyeicosatetraenoic acid, 4.5% 8-hydroxyeicosatetraenoic acid and 4.5% 15-hydroxyeicosatetraenoic acid. 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. No activity detected with 1-palmitoyl-2-linoleoylphosphatidylcholine. A model is tested that predicts a relationship between substrate binding orientation and product stereochemistry
Products: -
Products: -
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additional information
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Substrates: from arachidonate the wild-type enzyme forms 47% 11-hydroxyeicosatetraenoic acid, 23% 5-hydroxyeicosatetraenoic acid, 11% 9-hydroxyeicosatetraenoic acid, 9% 12-hydroxyeicosatetraenoic acid, 4.5% 8-hydroxyeicosatetraenoic acid and 4.5% 15-hydroxyeicosatetraenoic acid. 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. No activity detected with 1-palmitoyl-2-linoleoylphosphatidylcholine. A model is tested that predicts a relationship between substrate binding orientation and product stereochemistry
Products: -
Products: -
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additional information
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Substrates: arachidonic acid is a poor substrate
Products: -
Products: -
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additional information
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Substrates: arachidonic acid is a poor substrate
Products: -
Products: -
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additional information
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Substrates: arachidonic acid is a poor substrate
Products: -
Products: -
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additional information
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Substrates: low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
Products: -
Products: -
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additional information
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Substrates: low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
Products: -
Products: -
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additional information
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Substrates: in chitosan-treated Adelostemma gracillimum seedlings 9-LOX-derived oxylipins, namely 9,10,11-trihydroxy-12-octadecenoic acid, accumulate
Products: -
Products: -
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additional information
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Substrates: in chitosan-treated Adelostemma gracillimum seedlings 9-LOX-derived oxylipins, namely 9,10,11-trihydroxy-12-octadecenoic acid, accumulate
Products: -
Products: -
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additional information
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Substrates: the enzyme converted linoleic and linolenic acids almost exclusively to their 9-hydroperoxides
Products: -
Products: -
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additional information
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Substrates: the enzyme converted linoleic and linolenic acids almost exclusively to their 9-hydroperoxides
Products: -
Products: -
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additional information
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Substrates: regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX
Products: -
Products: -
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additional information
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Substrates: regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX
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additional information
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Substrates: Nb-9-LOX possesses both 9-lipoxygenase and 13-lipoxygenase, EC 1.13.11.12, specificity, with high predominance for the 9-LOX function
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additional information
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Substrates: from arachidonate the wild-type enzyme forms 11-hydroxyeicosatetraenoic acid and 5-hydroxyeicosatetraenoic acid in essentially equal amounts (38-39%), 11% 8-hydroxyeicosatetraenoic acid, 4% 12-hydroxyeicosatetraenoic acid, 3% 15-hydroxyeicosatetraenoic acid and 2% 9-hydroxyeicosatetraenoic acid. 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%). No activity detected with 1-palmitoyl-2-linoleoylphosphatidylcholine. A model is tested that predicts a relationship between substrate binding orientation and product stereochemistry
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additional information
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Substrates: from arachidonate the wild-type enzyme forms 11-hydroxyeicosatetraenoic acid and 5-hydroxyeicosatetraenoic acid in essentially equal amounts (38-39%), 11% 8-hydroxyeicosatetraenoic acid, 4% 12-hydroxyeicosatetraenoic acid, 3% 15-hydroxyeicosatetraenoic acid and 2% 9-hydroxyeicosatetraenoic acid. 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%). No activity detected with 1-palmitoyl-2-linoleoylphosphatidylcholine. A model is tested that predicts a relationship between substrate binding orientation and product stereochemistry
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additional information
?
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Substrates: low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
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additional information
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Substrates: low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
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additional information
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Substrates: the enzyme catalyzes oxygenation at the n-12 position of C20 and C22 polyunsaturated fatty acids to form 9S- and 11S-hydroperoxy fatty acids, which are reduced to 9S- and 11S-hydroxy fatty acids by cysteine, respectively, and it catalyzes again oxygenation at the n-6 position of 11S-hydroxy fatty acids to form 9S,15S- and 11S,17S-dihydroxy fatty acids, respectively
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
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alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
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?
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
Substrates: -
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?
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
-
Substrates: -
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?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
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linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
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?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
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?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
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linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
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?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
Substrates: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
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Substrates: regiospecificity of Nb-9-LOX, overview
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Substrates: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
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Substrates: -
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
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Substrates: -
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additional information
?
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Substrates: in chitosan-treated Adelostemma gracillimum seedlings 9-LOX-derived oxylipins, namely 9,10,11-trihydroxy-12-octadecenoic acid, accumulate
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additional information
?
-
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Substrates: in chitosan-treated Adelostemma gracillimum seedlings 9-LOX-derived oxylipins, namely 9,10,11-trihydroxy-12-octadecenoic acid, accumulate
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additional information
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-
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Substrates: Nb-9-LOX possesses both 9-lipoxygenase and 13-lipoxygenase, EC 1.13.11.12, specificity, with high predominance for the 9-LOX function
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[5-(2-phenyl-1H-indol-3-yl)-3-(pyridin-3-yl)-4,5-dihydro-1H-pyrazol-1-yl]ethan-1-one
-
2-phenyl-3-[3-(pyridin-3-yl)-4,5-dihydro-1H-pyrazol-5-yl]-1H-indole
most potent inhibitor tested
ethyl 2-[(2E)-2-benzylidenehydrazinyl]-4-methyl-1,3-thiazole-5-carboxylate
compound exhibits dual inhibitory activity against both 15-LOX and bovine carbonic anhydrase II
ethyl 4-methyl-2-[(2E)-2-[(3-nitrophenyl)methylidene]hydrazinyl]-1,3-thiazole-5-carboxylate
-
additional information
not inhibitory: O-geranyl substituents at positions 5 and 6 of 3-acetylcoumarin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Specific adduction of plant lipid transfer protein by an allene oxide generated by 9-lipoxygenase and allene oxide synthase.
Infections
Differential modulation of the lipoxygenase cascade during typical and latent Pectobacterium atrosepticum infections.
Infections
Identification of MAPKs as signal transduction components required for the cell death response during compatible infection by the synergistic pair Potato virus X-Potato virus Y.
Infections
Lipid peroxidation during the hypersensitive response in potato in the absence of 9-lipoxygenases.
Infections
Oxylipin biosynthesis genes positively regulate PCD during compatible infections by the synergistic pair Potato virus X-Potato virus Y and by Tomato spotted wilt virus.
Infections
Oxylipins from both pathogen and host antagonize jasmonic acid-mediated defence via the 9-lipoxygenase pathway in Fusarium verticillioides infection of maize.
Infections
Reduction of divinyl ether-containing polyunsaturated fatty acids in transgenic potato plants.
Infections
The pepper 9-lipoxygenase gene CaLOX1 functions in defense and cell death responses to microbial pathogens.
Infections
The pepper lipoxygenase CaLOX1 plays a role in osmotic, drought, and high salinity.
Infections
Transcriptional Changes of Plant Defense-Related Genes in Response to Clavibacter Infection in Pepper and Tomato.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00456
1-[5-(2-phenyl-1H-indol-3-yl)-3-(pyridin-3-yl)-4,5-dihydro-1H-pyrazol-1-yl]ethan-1-one
Glycine max
pH not specified in the publication, temperature not specified in the publication
0.00384
2-phenyl-3-[3-(pyridin-3-yl)-4,5-dihydro-1H-pyrazol-5-yl]-1H-indole
Glycine max
pH not specified in the publication, temperature not specified in the publication
0.00489
2-phenyl-3-[3-(pyridin-4-yl)-4,5-dihydro-1,2-oxazol-5-yl]-1H-indole
Glycine max
pH not specified in the publication, temperature not specified in the publication
0.018
4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
Glycine max
pH 7, 30°C
-
0.00012
ethyl 2-[(2E)-2-benzylidenehydrazinyl]-4-methyl-1,3-thiazole-5-carboxylate
Glycine max
pH 8.0, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
pH 5.0: about 50% of maximal activity, pH 7: about 70% of maximal activity
5 - 7.5
over 80% of maximal activity in a broad pH range with sharply decreasing relative activity below pH 5.0 and above pH 7.5
5 - 8.5
pH 5.0: about 50% of maximal activity, pH 8.5: 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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
-
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
15 - 55
isozyme LOX1:Md:1c displays high catalytic activity in a broad range of temperatures between 15°C and 50°C, with a sharp decrease above 50°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected in Shangrila County, Yunnan Province, China, gene AgLOX1
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
brenda
additional information
expression of CaLOX1 is differentially induced in pepper leaves not only during Xanthomonas campestris pv. vesicatoria infection but also after exposure to abiotic elicitors. Transient expression of CaLOX1 in pepper leaves induces the cell death phenotype and defense responses
brenda
-
expression of CaLOX1 is differentially induced in pepper leaves not only during Xanthomonas campestris pv. vesicatoria infection but also after exposure to abiotic elicitors. Transient expression of CaLOX1 in pepper leaves induces the cell death phenotype and defense responses
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brenda
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
brenda
not expressed in untreated leaves, but displays differential induction by defense-related hormones
brenda
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
brenda
the expression level of the r9-LOX1 gene is higher in imbibed seeds rather than developing seeds
brenda
ZmLOX5 is strongly inducible in leaves and stems by wounding but not in roots
brenda
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
brenda
additional information
-
enzyme production and activity level gradually increases with temperature, peaking at 30-35°C after both two and three weeks
brenda
additional information
-
enzyme production and activity level gradually increases with temperature, peaking at 30-35°C after both two and three weeks
-
brenda
additional information
no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development
brenda
additional information
-
no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development
brenda
additional information
cultivar/tissue specific expression of L-2, the expression is generally much higher in active bran/seed than in stabilized bran, mature seeds, and regenerated plants
brenda
additional information
-
cultivar/tissue specific expression of L-2, the expression is generally much higher in active bran/seed than in stabilized bran, mature seeds, and regenerated plants
brenda
additional information
low constitutive expression of Osr9-LOX1 in rice leaves, stems, and spikelets, but high constitutive expression in roots, expression analysis
brenda
additional information
cultivar/tissue specific expression of r9-LOX1, the expression is generally much higher in active bran/seed than in stabilized bran, mature seeds, and regenerated plants
brenda
additional information
accumulation of LOX 1 class transcript is restricted to developing tubers, stolons, and roots correlating mRNA accumulation positively with tuber initiation and growth
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
DNA and amino acid sequence determination and analysis of LOX1 and LOX2 isozymes, phylogenetic analysis, only LOX1:Md:1a exhibits a glycine residue (Gly567) responsible for dual positional specificity and (R)-LOX activity
evolution
analysis of functional domains, families and motifs along with the phylogenetic analysis
malfunction
CaLOX1-silenced pepper plants are more susceptible to Xanthomonas campestris pv. vesicatoria and Colletotrichum coccodes infection
malfunction
-
inactivation of ZmLOX3 results not only in reduced levels of fumonisin production and decreased conidiation of Fusarium verticillioides but also in decreased disease severity caused by distantly related fungal pathogens Colletotrichum graminicola and Cochliobolus heterostrophus. Hypothesis: certain fungi may require host plant 9-LOX-derived oxylipins to upregulate their developmental processes such as conidiation and mycotoxin production. Although 9-LOX derived oxylipins are reduced in the lox3-4 mutant, no significant differences of 13-LOX products derived from either C18:2 or C18:3 are observed between the embryos of wild types and lox3-4 mutants
malfunction
mutants that lack LOX1 and LOX5 function develop more emergent (stage VIII) and lateral roots than wild-type plants
malfunction
-
partial impairment of lox1 and dox1, encoding 9-lipoxygenase and alpha-dioxygenase, mutants to activate systemic acquired resistance against virulent Pseudomonas syringae pv. tomato strain Pst DC3000, enhanced susceptibility of lox1 to the virulent Pseudomonas syringae pv. tomato strain Pst DC3000. 9-Ketooctadecatrienoic acid levels are reduced in lox1 and lox1 dox1 plants but strongly increased in the dox1 mutant due to metabolic interaction of the two pathways. Mutant lox1 dox1 seedlings are hypersensitive to the growth-inhibitory effect of abscisic acid and show enhanced activation of abscisic acid-inducible marker genes as compared with wild-type plants. Phenotypes, overview
malfunction
antisense expression of Osr9-lox1 (asr9lox1) decrease the amount of wound-induced (Z)-3-hexenal but increase levels of striped stem borer (SSB)-induced linolenic acid, jasmonic acid, salicylic acid and trypsin protease inhibitors. These changes are associated with increased resistance in rice to the larvae of the SSB Chilo suppressalis. Silencing Osr9-LOX1 results in increased jasmonic acid, salicylic acid and green leaf volatiles ((Z)-3-hexenal) levels
malfunction
-
enzyme mutants are more resistant to infections with Fusarium verticillioides
malfunction
-
CaLOX1-silenced pepper plants are more susceptible to Xanthomonas campestris pv. vesicatoria and Colletotrichum coccodes infection
-
metabolism
-
plant 9-lipoxygenases and alpha-dioxygenases initiate the synthesis of oxylipins after bacterial infection. Pretreatment with 9-LOX- and alpha-DOX-generated oxylipins protected plant tissues against bacterial infection, especially 9-oxo-10(E),12(Z),15(Z)-octadecatrienoic acid, which is produced from linolenic acid by 9-LOX
metabolism
-
9-lipoxygenase-generated fatty acid hydroperoxides are converted into specific trihydroxy acids by the EAS-epoxide hydrolase pathway in the beetroot. The linolenic acid-derived hydroperoxide 9(S)-hydroperoxy-10(E),12(Z),15(Z)-octadecatrienoic acid is converted into 9(S),12(S),13(S)-trihydroxy-10(E),15(Z)-octadecadienoic acid (fulgidic acid). On the other hand, the 13-lipoxygenase-generated hydroperoxides of linoleic or linolenic acids fail to produce significant amounts of trihydroxy acids. Short-time incubation of 9(S)-hydroperoxy-10(E),12(Z)-octadecadienoic acid affords the epoxy alcohol 12(R),13(S)-epoxy-9(S)-hydroxy-10(E)-octadecenoic acid as the main product indicating the sequence 9-hydroperoxide to epoxy alcohol to trihydroxy acid catalyzed by epoxy alcohol synthase and epoxide hydrolase activities, respectively
physiological function
putative role for this gene in defense against insects
physiological function
CaLOX1 positively regulates defense and cell death responses to microbial pathogens
physiological function
-
ZmLOX3 is required for normal plant development. The ZmLOX3-mediated pathway may act as a root-specific suppressor of all three major defense signaling pathways to channel plant energy into growth processes, but is required for normal levels of resistance against nematodes
physiological function
enzyme is involved in cell death during cotton hypersensitive reaction
physiological function
LOX1 and LOX5 may function as regulators of root development by controlling the emergence of lateral roots through the production of (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
physiological function
chitosan-induced AgLOX1 encodes a 9-lipoxygenase potentially involved in the defense response through 9-LOX pathway leading to biosynthesis of antimicrobial compounds in Adelostemma gracillimum seedlings
physiological function
-
the LOX1 pathway is involved in regulating abscisic acid responses
physiological function
lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus domestica) fruit upon tissue disruption, role in autonomously produced aroma volatiles from intact tissue, overview. The genetic association with a quantitative trait locus for fruit ester and the remarkable agreement in regio- and stereoselectivity of the LOX1:Md:1a reaction with the overall LOX activity found in mature apple fruits, suggest a major physiological function of LOX1:Md:1a during climacteric ripening of apples. While isozymes LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b may contribute to aldehyde production in immature fruit upon cell disruption isozyme, LOX1:Md:1a probably regulates the availability of precursors for ester production in intact fruit tissue. Both 9- and 13-hydroperoxides can be catabolized to aroma-active volatile aldehydes by hydroperoxide lyase. Only 13-LOX activity contributes to the apple aroma due to the formation of precursors of C6 volatile compounds. The dioxygenation of PUFAs by 9- and 13-LOX activity forms precursors for important phytooxylipins with functions in plant defense, wound signaling, senescence and fruit ripening
physiological function
enzyme Osr9-LOX1 plays an important role in regulating an herbivore-induced jasmonic acid burst and cross-talk between jasmonic acid and salicylic acid, and in controlling resistance in rice to chewing and phloem-feeding herbivores
physiological function
r9-LOX1 positively regulates the amount of nonanal but negatively regulates acetic acid and hexanal. The negative regulation may be due to a mechanism of negative feedback between LOX family members
physiological function
the tuberization protein linoleate 9S-lipoxygenase 3 is not the only gene responsible for tuberization in potato. Tuber formation process regulation, overview
physiological function
-
the enzyme plays an important role in hormonal stress response during fruit ripening
physiological function
-
the enzyme is a major susceptibility factor induced by fungal linoleate diol synthase 1-derived oxylipins to suppress jasmonate-stimulating 9-lipoxygenases. Enzyme-mediated signaling promotes the biosynthesis of virulence-promoting oxylipins in Fusarium verticillioides. Host enzyme-produced oxylipins are essential for the normal infection and colonization processes of maize seed by Fusarium verticillioides
physiological function
-
CaLOX1 positively regulates defense and cell death responses to microbial pathogens
-
Show AA Sequence and Transmembrane Helices (122 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110700
x * 98000, about, sequence calculation, x * 110700, recombinant His-tagged enzyme, SDS-PAGE
98000
98000
x * 98000, about, sequence calculation, x * 110700, recombinant His-tagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
primary and secondary structure analysis of linoleate 9S-lipoxygenase 3, domain structure, especially the PLAT domain that forms a beta-sandwich composed of two sheets of four strands each, overview
?
x * 98000, about, sequence calculation, x * 110700, recombinant His-tagged enzyme, SDS-PAGE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
docking of inhibitor 7-farnesyloxy-3-acetylcoumarin exhibits pi-pi-interaction between Phe576 and the aromatic ring of coumarin, the carbonyl group in the pyranone ring and acetyl group are able to make a hydrogen bond with the side chain of His513 and Ser510 residues
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A562G
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
-
the mutant reacts well with arachidonic acid even in the absence of fatty acid hydroperoxides
G567A
site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation
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%)
I395F
-
the regioselectivity of the variant is changed from the n-12 position on C20 PUFA to the n-6 position to form 15S-HFAs
V569W
-
the variant has a significantly lower secondx1eoxygenating activity compared to wild type enzyme
additional information
additional information
in transgenic lines, L-2, expression is dramatically downregulated, compared to the nontransgenic controls, enzyme knockout in Oryza sativa by hpRNAi expression, transfection via Agrobacterium tumefaciens strain EHA105
additional information
-
in transgenic lines, L-2, expression is dramatically downregulated, compared to the nontransgenic controls, enzyme knockout in Oryza sativa by hpRNAi expression, transfection via Agrobacterium tumefaciens strain EHA105
additional information
antisense expression of Osr9-lox1 (asr9lox1), by Agrobacterium tumefaciens-mediated transformation, decrease the amount of wound-induced (Z)-3-hexenal but increase levels of striped stem borer (SSB)-induced linolenic acid, lasmonic acid, salicylic acid and trypsin protease inhibitors
additional information
enzyme knockout in Oryza sativa by hpRNAi expression, transfection via Agrobacterium tumefaciens strain EHA105, in transgenic lines, r9-LOX1 expression is dramatically downregulated, compared to the nontransgenic controls. r9-LOX1 RNAi transgenic lines show 74.33% decrease in nonanal content (formed during oxidation of linoleic acid by lipoxygenase), but a 388.24% increase in acetic acid and 184.84% hexanal (direct products of 13-LOX)
additional information
expression of antisense coding sequence of a specific tuber LOX, the suppression mutant POTLX-1 exhibits a significant reduction in LOX activity in stolons and tubers
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially purified by nickel affinity chromatography using a N-terminal (His)6-tag
recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration
recombinnat enzyme partially from Escherichia coli by nickel affinity chromatography
partially purified by nickel affinity chromatography using a N-terminal (His)6-tag
partially purified by nickel affinity chromatography using a N-terminal (His)6-tag
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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
gene AgLOX1, cloned from chitosan-induced seedling, DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
gene lox1, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis, recombinant expression of EGFP-tagged enzyme in Nicotiana tabacum under control of the the CaMV35S promoter
gene lox1, DNA and amino acid sequence determination and analysis, realtime PCR expression analysis, the gene shows a cultivar/tissue specific expression
gene LOX1.1, DNA and amino acid sequence determination and analysis, realtime PCR expression analysis, the gene shows a cultivar/tissue specific expression
gene LOX1.3, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
gene LOX1c, RT-PCR and real-time quantitative PCR expression analysis, 22 putative LOX genes in apple, gene expression analysis throughout ripening reveals that only six LOXs are expressed in a ripening-dependent manner, overview. DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged or untagged LOX genes endoing for isozymes LOX1:Md:1a, L, X1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b, containing an enterokinase cleavage recognition site in the first case, in Saccharomyces cerevisiae strain INVSc1
gene Nb-9-LOX, DNA and amino acid sequence determination and analysis, overexpression in Saccharomyces cerevisiae, quantitative realtime PCR exxpression analysis
-
heterologously expressed in Escherichia coli
overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is evidently suppressed in cultivar Fupingjianshi fruit treated with 0.1 mM salicylic acid for 10 min
-
expression of a maize 9-LOX gene, ZmLOX3, increases steadily and peaks at 7 days after inoculation with Meloidogyne incognita root-knot nematodes
-
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
herbivore infestation, mechanical wounding and jasmonic acid treatment either repress or do not enhance the level of Osr9-LOX1 transcripts at early stages but do at later stages
herbivore infestation, mechanical wounding and jasmonic acid treatment either repress or do not enhance the level of Osr9-LOX1 transcripts at early stages but do at later stages, whereas salicylic acid (SA) treatment quickly increases the transcript level of Osr9-LOX1
isoform LOX1 expression is considerably downregulated at low temperature (4°C). Isoforms LOX2 and LOX5 are considerably downregulated by low (4°C) and high (40°C) temperature, and NaCl treatment
-
isoforms LOX1, 2, 8, and 14 are immediately downregulated by heat stress. Isoform LOX2 is immediately downregulated by cold stress. Isoforms LOX2, 5, 7, 8, 13, and 14 are immediately downregulated by salt stress. Isoforms LOX5 and 7 are immediately downregulated by drought stress
-
isoforms LOX5, 6, 7, and 13 are immediately upregulated by heat stress. Isoforms LOX1, 6, 7, 8, 13, and 14 are immediately upregulated by cold stress. Isoforms LOX1, 6, and 9 are immediately upregulated by salt stress. Isoforms LOX1, 2, 6, 7, 8, 9, and 13 are immediately upregulated by drought stress
-
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
-
the enzyme expression in cultivar Fupingjianshi increases sharply and reaches a peak on the same day (12 days) as ethylene production, then decreases towards the late stages of ripening. The expression level in cultivar Ganmaokui also increases several-fold during late ripening, reaching a maximum at 20 days after harvest. Enzyme expression is stimulated strongly in cultivar Fupingjianshi fruit treated with 0.189 mM abscisic acid for 2 min
-
the enzyme expression is highly induced by agroinfiltration of the plant leaves using a tobacco mosaic virus based vector system
-
the enzyme is induced by low molecular weight chitosan, expression pattern, overview
the expression levels of all isoforms are not affected by the Plasmodiophora brassicae infection
-
transcripts of ZmLOX5 are increased in response to jasmonic acid and salicylic acid treatments. ZmLOX5 is transiently induced both locally and systemically by wounding
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
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
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme could be useful for in vitro synthesis of 9,10-ketol-octadecadienoic acid which is expected to be an ornamentally useful flower inducer when applied exogenously
synthesis
-
the yeast expressed Nb-9-LOX can be used to produce C9-aldehydes on a large scale in combination with a HPL gene with 9-hydroperoxide lyase function, or to effectively produce 9-hydroxy-10(E),12(Z)-octadecadienoic acid in a biocatalytic process in combination with cysteine as a mild reducing agent
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doderer, A.; Kokkelink, I.; van der Veen, S.; Valk, B.E.; Schram, A.W.; Douma, A.C.
Purification and characterization of two lipoxygenase isoenzymes from germinating barley
Biochim. Biophys. Acta
1120
97-104
1992
Hordeum vulgare (P29114)
brenda
Kuo, J.M.; Hwang, A.; Yeh, D.B.; Pan, M.H.; Tsai, M.L.; Pan, B.S.
Lipoxygenase from banana leaf: purification and characterization of an enzyme that catalyzes linoleic acid oxygenation at the 9-position
J. Agric. Food Chem.
54
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2006
Musa acuminata
brenda
Garbe, L.A.; Barbosa de Almeida, R.; Nagel, R.; Wackerbauer, K.; Tressl, R.
Dual positional and stereospecificity of lipoxygenase isoenzymes from germinating barley (green malt): biotransformation of free and esterified linoleic acid
J. Agric. Food Chem.
54
946-955
2006
Hordeum vulgare (P29114)
brenda
Chechetkin, I.R.; Osipova, E.V.; Tarasova, N.B.; Mukhitova, F.K.; Hamberg, M.; Gogolev, Y.V.; Grechkin, A.N.
Specificity of oxidation of linoleic acid homologs by plant lipoxygenases
Biochemistry
74
855-861
2009
Zea mays
brenda
Mita, G.; Gallo, A.; Greco, V.; Zasiura, C.; Casey, R.; Zacheo, G.; Santino, A.
Molecular cloning and biochemical characterization of a lipoxygenase in almond (Prunus dulcis) seed
Eur. J. Biochem.
268
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2001
Prunus dulcis (Q9LEA9), Prunus dulcis Mill. (Q9LEA9)
brenda
Royo, J.; Vancanneyt, G.; Perez, A.G.; Sanz, C.; Strmann, K.; Rosahl, S.; Sanchez-Serrano, J.J.
Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns
J. Biol. Chem.
271
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1996
Solanum tuberosum (P37831)
brenda
Hamberg M.
Isolation and structures of two divinyl ether fatty acids from Clematis vitalba
Lipids
39
565-569
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Clematis vitalba
brenda
Boeglin, W.E.; Itoh, A.; Zheng, Y.; Coffa, G.; Howe, G.A.; Brash, A.R.
Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases
Lipids
43
979-987
2008
Arabidopsis thaliana (Q06327), Arabidopsis thaliana, Solanum lycopersicum (P38415), Solanum lycopersicum
brenda
Andreou, A.Z.; Hornung, E.; Kunze, S.; Rosahl, S.; Feussner, I.
On the substrate binding of linoleate 9-lipoxygenases
Lipids
44
207-215
2008
Arabidopsis thaliana (Q06327), Arabidopsis thaliana, Solanum tuberosum (P37831), Solanum tuberosum
brenda
Bannenberg, G.; Martnez, M.; Hamberg, M.; Castresana, C.
Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana
Lipids
44
85-95
2008
Arabidopsis thaliana (Q06327), Arabidopsis thaliana (Q9LUW0), Arabidopsis thaliana
brenda
Gao, X.; Shim, W.B.; Gbel, C.; Kunze, S.; Feussner, I.; Meeley, R.; Balint-Kurti, P.; Kolomiets, M.
Disruption of a maize 9-lipoxygenase results in increased resistance to fungal pathogens and reduced levels of contamination with mycotoxin fumonisin
Mol. Plant Microbe Interact.
20
922-933
2007
Zea mays
brenda
Gao, X.; Starr, J.; Gbel, C.; Engelberth, J.; Feussner, I.; Tumlinson, J.; Kolomiets, M.
Maize 9-lipoxygenase ZmLOX3 controls development, root-specific expression of defense genes, and resistance to root-knot nematodes
Mol. Plant Microbe Interact.
21
98-109
2008
Zea mays
brenda
Mizuno, K.; Iida, T.; Takano, A.; Yokoyama, M.; Fujimura, T.
A new 9-lipoxygenase cDNA from developing rice seeds
Plant Cell Physiol.
44
1168-1175
2003
Oryza sativa (Q76I22), Oryza sativa
brenda
Vellosillo, T.; Martnez, M.; Lopez, M.A.; Vicente, J.; Cascon, T.; Dolan, L.; Hamberg, M.; Castresana, C.
Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
Plant Cell
19
831-846
2007
Arabidopsis thaliana (Q06327), Arabidopsis thaliana (Q9LUW0), Arabidopsis thaliana
brenda
Marmey, P.; Jalloul, A.; Alhamdia, M.; Assigbetse, K.; Cacas, J.L.; Voloudakis, A.E.; Champion, A.; Clerivet, A.; Montillet, J.L.; Nicole, M.
The gene is associated with the hypersensitive reaction of cotton Gossypium hirsutum to Xanthomonas campestris pv malvacearum
Plant Physiol. Biochem.
45
596-606
2007
Gossypium hirsutum (Q93WZ2), Gossypium hirsutum
brenda
Hwang, I.S.; Hwang, B.K.
The pepper 9-lipoxygenase gene CaLOX1 functions in defense and cell death responses to microbial pathogens
Plant Physiol.
152
948-967
2010
Capsicum annuum (D3TTH9), Capsicum annuum Nockwang (D3TTH9)
brenda
Ben-Hayyim, G.; Gueta-Dahan, Y.; Avsian-Kretchmer, O.; Weichert, H.; Feussner, I.
Preferential induction of a 9-lipoxygenase by salt in salt-tolerant cells of Citrus sinensis L. Osbeck
Planta
212
367-375
2001
Citrus sinensis
brenda
Park, Y.S.; Kunze, S.; Ni, X.; Feussner, I.; Kolomiets, M.V.
Comparative molecular and biochemical characterization of segmentally duplicated 9-lipoxygenase genes ZmLOX4 and ZmLOX5 of maize
Planta
231
1425-1437
2010
Zea mays (A1XCI0), Zea mays
brenda
Huang, F.C.; Schwab, W.
Cloning and characterization of a 9-lipoxygenase gene induced by pathogen attack from Nicotiana benthamiana for biotechnological application
BMC Biotechnol.
11
30
2011
Nicotiana benthamiana
brenda
Li, J.; Zhao, P.J.; Ma, C.L.; Zeng, Y.
A chitosan induced 9-lipoxygenase in Adelostemma gracillimum seedlings
Int. J. Mol. Sci.
13
540-551
2012
Cynanchum gracillimum (Q4FCM5), Cynanchum gracillimum
brenda
Nam, K.H.; Yoshihara, T.
Interactions among LOX metabolites regulate temperature-mediated flower bud formation in morning glory (Pharbitis nil)
J. Plant Physiol.
169
1815-1820
2012
Ipomoea nil, Ipomoea nil Choisy
brenda
Hamberg, M.; Olsson, U.
Efficient and specific conversion of 9-lipoxygenase hydroperoxides in the beetroot. Formation of pinellic acid
Lipids
46
873-878
2011
Beta vulgaris
brenda
Vicente, J.; Cascon, T.; Vicedo, B.; Garcia-Agustin, P.; Hamberg, M.; Castresana, C.
Role of 9-lipoxygenase and alpha-dioxygenase oxylipin pathways as modulators of local and systemic defense
Mol. Plant
5
914-928
2012
Arabidopsis thaliana
brenda
Zheng, Y.; Brash, A.R.
Dioxygenase activity of epidermal lipoxygenase-3 unveiled: typical and atypical features of its catalytic activity with natural and synthetic polyunsaturated fatty acids
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285
39866-39875
2010
Homo sapiens
brenda
Roychowdhury, M.; Li, X.; Qi, H.; Li, W.; Sun, J.; Huang, C.; Wu, D.
Functional characterization of 9-/13-LOXs in rice and silencing their expressions to improve grain qualities
BioMed Res. Int.
2016
4275904
2016
Oryza sativa (P29250), Oryza sativa, Oryza sativa Japonica Group (Q76I22)
brenda
Schiller, D.; Contreras, C.; Vogt, J.; Dunemann, F.; Defilippi, B.G.; Beaudry, R.; Schwab, W.
A dual positional specific lipoxygenase functions in the generation of flavor compounds during climacteric ripening of apple
Hortic. Res.
2
15003-15015
2015
Malus domestica (S4UL39), Malus domestica
brenda
Rameshwari, R.; Madhu, S.; Prasad, V.; Chapadgaonkar, S.
Computational analysis of tuberization protein linoleate 9S-lipoxygenase 3 from Solanum tuberosum
Int. J. ChemTech Res.
8
294-310
2015
Solanum tuberosum (Q43189)
-
brenda
Zhou, G.; Ren, N.; Qi, J.; Lu, J.; Xiang, C.; Ju, H.; Cheng, J.; Lou, Y.
The 9-lipoxygenase Osr9-LOX1 interacts with the 13-lipoxygenase-mediated pathway to regulate resistance to chewing and piercing-sucking herbivores in rice
Physiol. Plant.
152
59-69
2014
Oryza sativa Japonica Group (Q76I22)
brenda
Saeed, A.; Khan, S.U.; Mahesar, P.A.; Channar, P.A.; Shabir, G.; Iqbal, J.
Substituted (E)-2-(2-benzylidenehydrazinyl)-4-methylthiazole-5-carboxylates as dual inhibitors of 15-lipoxygenase & carbonic anhydrase II synthesis, biochemical evaluation and docking studies
Biochem. Biophys. Res. Commun.
482
176-181
2017
Glycine max (P09186)
brenda
Kim, S.E.; Lee, J.; An, J.U.; Kim, T.H.; Oh, C.W.; Ko, Y.J.; Krishnan, M.; Choi, J.; Yoon, D.Y.; Kim, Y.; Oh, D.K.
Regioselectivity of an arachidonate 9S-lipoxygenase from Sphingopyxis macrogoltabida that biosynthesizes 9S,15S- and 11S,17S-dihydroxy fatty acids from C20 and C22 polyunsaturated fatty acids
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1867
159091
2022
Sphingopyxis macrogoltabida
brenda
Zerangnasrabad, S.; Jabbari, A.; Khavari Moghadam, E.; Sadeghian, H.; Seyedi, S.M.
Design, synthesis, and structure-activity relationship study of O-prenylated 3-acetylcoumarins as potent inhibitors of soybean 15-lipoxygenase
Drug Dev. Res.
82
826-834
2021
Glycine max (P09186)
brenda
ElBordiny, H.S.; El-Miligy, M.M.; Kassab, S.E.; Daabees, H.; Mohamed Ali, W.A.; Abdelhamid Mohamed El-Hawash, S.
Design, synthesis, biological evaluation and docking studies of new 3-(4,5-dihydro-1H-pyrazol/isoxazol-5-yl)-2-phenyl-1H-indole derivatives as potent antioxidants and 15-lipoxygenase inhibitors
Eur. J. Med. Chem.
145
594-605
2018
Glycine max (P09186)
brenda
Upadhyay, R.K.; Handa, A.K.; Mattoo, A.K.
Transcript abundance patterns of 9- and 13-lipoxygenase subfamily gene members in response to abiotic stresses (heat, cold, drought or salt) in tomato (Solanum lycopersicum L.) highlights member-specific dynamics relevant to each stress
Genes (Basel)
10
683
2019
Solanum lycopersicum
brenda
Meng, K.; Hou, Y.; Han, Y.; Ban, Q.; He, Y.; Suo, J.; Rao, J.
Exploring the functions of 9-lipoxygenase (DkLOX3) in ultrastructural changes and hormonal stress response during persimmon fruit storage
Int. J. Mol. Sci.
18
589
2017
Diospyros kaki
brenda
Wang, J.; Hu, T.; Wang, W.; Hu, H.; Wei, Q.; Wei, X.; Bao, C.
Bioinformatics analysis of the lipoxygenase gene family in radish (Raphanus sativus) and functional characterization in response to abiotic and biotic stresses
Int. J. Mol. Sci.
20
6095
2019
Raphanus sativus
brenda
An, J.U.; Lee, I.G.; Ko, Y.J.; Oh, D.K.
Microbial synthesis of linoleate 9S-lipoxygenase derived plant C18 oxylipins from C18 polyunsaturated fatty acids
J. Agric. Food Chem.
67
3209-3219
2019
Myxococcus xanthus, Myxococcus xanthus DK1622
brenda
Battilani, P.; Lanubile, A.; Scala, V.; Reverberi, M.; Gregori, R.; Falavigna, C.; Dallasta, C.; Park, Y.S.; Bennett, J.; Borrego, E.J.; Kolomiets, M.V.
Oxylipins from both pathogen and host antagonize jasmonic acid-mediated defence via the 9-lipoxygenase pathway in Fusarium verticillioides infection of maize
Mol. Plant Pathol.
19
2162-2176
2018
Zea mays
brenda
Deshpande, A.B.; Chidley, H.G.; Oak, P.S.; Pujari, K.H.; Giri, A.P.; Gupta, V.S.
Isolation and characterization of 9-lipoxygenase and epoxide hydrolase 2 genes Insight into lactone biosynthesis in mango fruit (Mangifera indica L.)
Phytochemistry
138
65-75
2017
Mangifera indica
brenda
Tolley, J.; Nagashima, Y.; Gorman, Z.; Kolomiets, M.; Koiwa, H.
Isoform-specific subcellular localization of Zea mays lipoxygenases and oxo-phytodienoate reductase 2
Plant Gene
13
36-41
2018
Zea mays
-
brenda
Woldemariam, M.; Ahern, K.; Jander, G.; Tzin, V.
A role for 9-lipoxygenases in maize defense against insect herbivory
Plant Signal. Behav.
13
e1422462
2018
Zea mays
brenda
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