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Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase and Organism(s) Solanum tuberosum and UniProt Accession P37831

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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 tuberosum
UNIPROT: P37831
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The taxonomic range for the selected organisms is: Solanum tuberosum
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
9-lipoxygenase
-
linoleate 9-lipoxygenase
-
linoleate 9S-lipoxygenase 3
-
tuberization protein
-
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
alpha-linolenate
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
-
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate is the main product
-
?
alpha-linolenate + O2
(10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
show the reaction diagram
-
96% (10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate and 2.1% (9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
?
gamma-linolenate + O2
(6Z,9S,10E,12Z)-9-hydroperoxy-6,10,12-octadecatrienoate
show the reaction diagram
-
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
-
?
linoleate + O2
(10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
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
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
show the reaction diagram
-
98% (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate, almost exclusively S stereoconfiguration. (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate is a minor byproduct
-
?
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
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
alpha-linolenic acid + O2
(10E,12Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
1 metal ion per subunit
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
Manually annotated by BRENDA team
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
Manually annotated by BRENDA team
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves
Manually annotated by BRENDA team
Lox1 transcripts are predominantly detected in tubers and roots and to a much lesser extent in buds and leaves. along tuber formation, Lox1 class transcripts are detected at the stolon stage, and their steady state levels increases during the early stages of tuber development
Manually annotated by BRENDA team
additional information
accumulation of LOX 1 class transcript is restricted to developing tubers, stolons, and roots correlating mRNA accumulation positively with tuber initiation and growth
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
analysis of functional domains, families and motifs along with the phylogenetic analysis
metabolism
the enzyme takes part in the LOX pathway, overview
physiological function
the tuberization protein linoleate 9S-lipoxygenase 3 is not the only gene responsible for tuberization in potato. Tuber formation process regulation, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOX11_SOLTU
861
0
96967
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
gene LOX1.3, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
21012-21009
1996
Solanum tuberosum (P37831)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team