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Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase and Organism(s) Solanum lycopersicum and UniProt Accession P38415

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IUBMB 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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Solanum lycopersicum
UNIPROT: P38415
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The taxonomic range for the selected organisms is: Solanum lycopersicum
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
linoleate 9S-lipoxygenase
-
9-lipoxygenase
-
-
LOX1
-
isoform
LOX13
-
isoform
LOX14
-
isoform
LOX2
-
isoform
LOX5
-
isoform
LOX6
-
isoform
LOX7
-
isoform
LOX8
-
isoform
LOX9
-
isoform
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
linoleate + O2
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
-
-
-
-
?
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 9
pH 8: 30% of optimal activity, pH 9: about 15% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOXA_SOLLC
860
0
96765
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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%)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially purified by nickel affinity chromatography using a N-terminal (His)6-tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologously expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform LOX9 is not influenced by heat or cold stress
-
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
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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
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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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team