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Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase and Organism(s) Arabidopsis thaliana and UniProt Accession Q06327
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1.13.11.58 linoleate 9S-lipoxygenaseIUBMB Comments
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 . EC 1.13.11.12 (linoleate 13S-lipoxygenase) catalyses a similar reaction at another position of these fatty acids.
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Word Map
- 1.13.11.58
-
linoleic
- oxylipins
-
9-loxs
- lipoxygenases
-
9s-hydroperoxide
-
13-lipoxygenase
-
divinyl
-
colneleic
-
trihydroxy
-
alpha-ketols
- epoxyalcohols
- 12r-lox
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9s-hydroperoxy-10e,12z-octadecadienoic
- synthesis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
9-lipoxygenase, zmlox3, r9-lox1, zmlox5, calox1, atlox1, epidermal lipoxygenase-3, ghlox1, nb-9-lox, linoleate 9s-lipoxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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.
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
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
-
-
?
alpha-linolenate + O2
?
comparable oxygenase activity with either linoleic acid or linolenic acid
no product determined
-
?
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
-
?
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
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
-
-
-
-
?
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
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
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
?
-
-
low activity with arachidonate, the C20 fatty acid is converted into a mixture of racemic products
-
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
(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
-
-
?
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
mutants that lack LOX1 and LOX5 function develop more emergent (stage VIII) and lateral roots than wild-type plants
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
malfunction
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
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
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
-
the LOX1 pathway is involved in regulating abscisic acid responses
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LOX1_ARATH
859
0
98045
Swiss-Prot
other Location (Reliability: 2)
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially purified by nickel affinity chromatography using a N-terminal (His)6-tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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