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Information on EC 1.13.11.12 - linoleate 13S-lipoxygenase and Organism(s) Hordeum vulgare and UniProt Accession P93184

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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 C-13 position with (S)-configuration. This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid. EC 1.13.11.58, linoleate 9S-lipoxygenase, catalyses a similar reaction at the second available position of these fatty acids.
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Hordeum vulgare
UNIPROT: P93184
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Word Map
The taxonomic range for the selected organisms is: Hordeum vulgare
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
lipoxygenase, 15-lipoxygenase-1, soybean lipoxygenase-1, lipoxygenase-1, 13-lox, 13-lipoxygenase, lox-2, lipoxygenase-2, lipoxygenase-3, lox10, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
linoleate:oxygen 13-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 C-13 position with (S)-configuration. This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid. EC 1.13.11.58, linoleate 9S-lipoxygenase, catalyses a similar reaction at the second available position of these fatty acids.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-60-1
-
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
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
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ratio of (9Z,11E,13S)-13-hydroperoxy-11,13-octadecadienoate to (9Z,11E,13R)-13-hydroperoxy-11,13-octadecadienoate is 93:7
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
-
trilinolein and extracted polar and nonpolar lipids are oxidized with a ratio (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate to (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate of 6:94, 2:98, and 7:93. The stereoisomer ratios (S:R) of (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate with these substrates are 82:18, 92:8, and 91:9 whereas (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is analyzed (R)-configured with 41:59, 47:53, and 40:60 (S:R)
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cadmium
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induces LOX activity. Cd-induced intracellular LOX activity increases equally along the barley root tip, while Cd-induced apoplastic LOX activity is associated mainly with the differentiation zone of the barley root tip. Cd-induced LOX activity in plants growing at 21°C increases with increasing temperatures
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
n-propyl gallate
-
causes a strong inhibition of the LOX-catalyzed enzymatic reaction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Salome
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
involvement of Cd-induced LOX activity in the premature differentiation of the barley root tip during Cd stress
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LOX21_HORVU
936
0
105864
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106000
x * 106000, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 106000, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cadmium induces lipoxygenase activity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Vrs, K.; Feussner, I.; Khn, H.; Lee, J.; Graner, A.; Lbler, M.; Parthier, B.; Wasternack, C.
Characterization of a methyljasmonate-inducible lipoxygenase from barley (Hordeum vulgare cv. Salome) leaves
Eur. J. Biochem.
251
36-44
1998
Hordeum vulgare (P93184), Hordeum vulgare
Manually annotated by BRENDA team
Tamas, L.; Dudikova, J.; Durcekova, K.; Haluskova, L.; Huttova, J.; Mistrik, I.
Effect of cadmium and temperature on the lipoxygenase activity in barley root tip
Protoplasma
235
17-25
2009
Hordeum vulgare
Manually annotated by BRENDA team