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Enzyme Nomenclature
Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase
for references in articles please use BRENDA:EC1.13.11.58
Word Map on EC 1.13.11.58
- 1.13.11.58
-
linoleic
- lipoxygenases
-
hydroperoxide
-
oxylipins
-
9s-hydroperoxide
-
13-lipoxygenase
-
alpha-ketols
-
colneleic
-
divinyl
-
trihydroxy
- 12r-lox
-
9s-hydroperoxy-10e,12z-octadecadienoic
-
epoxyalcohol
- synthesis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.13.11.58
-
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RECOMMENDED NAME
GeneOntology No.
linoleate 9S-lipoxygenase
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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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected in Shangrila County, Yunnan Province, China, gene AgLOX1
UniProt
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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
-
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; mutants that lack LOX1 and LOX5 function develop more emergent (stage VIII) and lateral roots than wild-type plants
malfunction
CaLOX1-silenced pepper plants are more susceptible to Xanthomonas campestris pv. vesicatoria and Colletotrichum coccodes infection
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
-
CaLOX1-silenced pepper plants are more susceptible to Xanthomonas campestris pv. vesicatoria and Colletotrichum coccodes infection
-
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
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
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
-
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; 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
enzyme is involved in cell death during cotton hypersensitive reaction
physiological function
CaLOX1 positively regulates defense and cell death responses to microbial pathogens
physiological function
putative role for this gene in defense against insects
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
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
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
the tuberization protein linoleate 9S-lipoxygenase 3 is not the only gene responsible for tuberization in potato. Tuber formation process regulation, overview
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
-
CaLOX1 positively regulates defense and cell death responses to microbial pathogens
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
-
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
-
-
36%, 22%, 21% and 13% yield, respectively
-
?
alpha-linolenate
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate is the main product
-
?
alpha-linolenate + O2
?
comparable oxygenase activity with either linoleic acid or linolenic acid
no product determined
-
?
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecaterieonoic acid
-
-
-
?
arachidonic acid + O2
5-HPETE + 7-HPETE + 9-HPETE
-
-
22%, 25% and 29% yield, respectively
-
?
gamma-linolenate + O2
(6Z,9S,10E,12Z)-9-hydroperoxy-6,10,12-octadecatrienoate
-
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
-
?
alpha-linolenate + O2
(10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
-
the R/S stereoconfiguration of the product is not determined
-
?
alpha-linolenate + O2
(10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
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
-
-
-
-
?
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
-
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
comparable oxygenase activity with either linoleic acid or linolenic acid
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
-
-
-
-
?
alpha-linolenate + O2
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
comparable oxygenase activity with either linoleic acid or linolenic acid
more than 96% of the substrate is converted to the the 9-positional hydroperoxide
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
-
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
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
-
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
-
-
the R/S stereoconfiguration of the product is not determined
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
(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
-
(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
linoleate (abundant in membrane lipids of tubers) is preferred to linolenate as substrate
the R/S stereoconfiguration of the product is not determined
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
recombinant ZmLOX5 protein displays clear 9-LOX regiospecificity at both neutral and slightly alkaline pH
the R/S stereoconfiguration of the product is not determined
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
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
-
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
-
oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
comparable oxygenase activity with either linoleic acid or linolenic acid
the enzyme forms exclusively (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
regiospecificity of Nb-9-LOX, overview
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
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)
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
the enzyme specifically forms the 9-H(p)ODE isomer by 99.5%, 97.7% of which is in S-form
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
regiospecificity of Nb-9-LOX, overview
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
comparable oxygenase activity with either linoleic acid or linolenic acid
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
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
-
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
-
9-lipoxygenase does not utilize docosadienoic acid and catalyzes eicosadienoic acid dioxygenation 20fold slower than linoleic acid dioxygenation
the enzyme specifically forms the S-stereoisomer
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
-
-
-
additional information
?
-
-
in chitosan-treated Adelostemma gracillimum seedlings 9-LOX-derived oxylipins, namely 9,10,11-trihydroxy-12-octadecenoic acid, accumulate
-
-
-
additional information
?
-
in chitosan-treated Adelostemma gracillimum seedlings 9-LOX-derived oxylipins, namely 9,10,11-trihydroxy-12-octadecenoic acid, accumulate
-
-
-
additional information
?
-
-
the enzyme converted linoleic and linolenic acids almost exclusively to their 9-hydroperoxides
-
-
-
additional information
?
-
the enzyme converted linoleic and linolenic acids almost exclusively to their 9-hydroperoxides
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
Nb-9-LOX possesses both 9-lipoxygenase and 13-lipoxygenase, EC 1.13.11.12, specificity, with high predominance for the 9-LOX function
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecaterieonoic acid
Q43189
-
-
-
?
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
alpha-linolenate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade
-
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
D3TTH9
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
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
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regiospecificity of Nb-9-LOX, overview
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
S4UL39
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linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
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additional information
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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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Q4FCM5
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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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
pH 5.0: about 50% of maximal activity, pH 8.5: 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 - 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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
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10°C: about 45% of maximal activity, 50°C: about 65% 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
15 - 30
15°C: about 90% of maximal activity, 30°C: about 40% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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
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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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Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
not expressed in untreated leaves, but displays differential induction by defense-related hormones
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
the expression level of the r9-LOX1 gene is higher in imbibed seeds rather than developing seeds
ZmLOX5 is strongly inducible in leaves and stems by wounding but not in roots
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
additional information
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enzyme production and activity level gradually increases with temperature, peaking at 30-35°C after both two and three weeks
additional information
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enzyme production and activity level gradually increases with temperature, peaking at 30-35°C after both two and three weeks
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additional information
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no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development
additional information
no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development
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
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
additional information
low constitutive expression of Osr9-LOX1 in rice leaves, stems, and spikelets, but high constitutive expression in roots, expression analysis
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
98000
110700
x * 98000, about, sequence calculation, x * 110700, recombinant His-tagged enzyme, SDS-PAGE
98000
x * 98000, about, sequence calculation, x * 110700, recombinant His-tagged enzyme, SDS-PAGE
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SUBUNITS
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
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x * 98000, about, sequence calculation, x * 110700, recombinant His-tagged enzyme, SDS-PAGE
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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
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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
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heterologously expressed in Escherichia coli
overexpression in Escherichia coli
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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
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
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
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
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%)
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
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
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
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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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
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.13.11.58)
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