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Information on EC 1.13.11.58 - linoleate 9S-lipoxygenase and Organism(s) Hordeum vulgare and UniProt Accession P29114

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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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Hordeum vulgare
UNIPROT: P29114
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Word Map
The taxonomic range for the selected organisms is: Hordeum vulgare
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
9-lipoxygenase, zmlox3, r9-lox1, zmlox5, calox1, atlox1, ghlox1, epidermal lipoxygenase-3, nb-9-lox, linoleate 9s-lipoxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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)
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
pH 5.0: about 50% of maximal activity, pH 8.5: about 70% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 5.3
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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?
LOX1_HORVU
862
0
96393
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
x * 90000, SDS-PAGE
93200
density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 90000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doderer, A.; Kokkelink, I.; van der Veen, S.; Valk, B.E.; Schram, A.W.; Douma, A.C.
Purification and characterization of two lipoxygenase isoenzymes from germinating barley
Biochim. Biophys. Acta
1120
97-104
1992
Hordeum vulgare (P29114)
Manually annotated by BRENDA team
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 (P29114)
Manually annotated by BRENDA team