Information on EC 1.13.11.12 - linoleate 13S-lipoxygenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.13.11.12
-
RECOMMENDED NAME
GeneOntology No.
linoleate 13S-lipoxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
(2)
-
-
-
linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
; (1)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
redox reaction
-
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
alpha-Linolenic acid metabolism
-
divinyl ether biosynthesis II
-
jasmonic acid biosynthesis
-
Linoleic acid metabolism
-
Metabolic pathways
-
traumatin and (Z)-3-hexen-1-yl acetate biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(13S)-lipoxygenase
-
-
(13S)-lipoxygenase
Ipomoea nil Choisy
-
-
-
13-lipoxygenase
-
-
13-lipoxygenase
Fusarium oxysporum 4287
-
-
-
13-lipoxygenase
-
-
13-lipoxygenase
-
-
13-lipoxygenase
-
-
13-lipoxygenase
-
-
13-LOX
-
-
13-LOX
Q6X5R5, Q6X5R6
-
13S-lipoxygenase
P38418, Q9CAG3, Q9FNX8, Q9LNR3
-
15-lipoxygenase-1
-
-
15-LOX-1
-
-
9/13-LOX
B6D1W5
-
AtLOX-2
P38418
-
AtLOX-3
Q9LNR3
-
AtLOX-4
Q9FNX8
-
AtLOX-6
Q9CAG3
-
iron 13S-lipoxygenase
-
-
iron 13S-lipoxygenase
Fusarium oxysporum 4287
-
-
-
liipoxygenase
-
-
liipoxygenase
Pseudomonas aeruginosa BBE
-
-
-
linoleate 13-lipoxygenase
B2IZG6
-
linoleate 13-lipoxygenase
Nostoc punctiforme PCC73102
B2IZG6
-
-
linoleate:oxygen oxidoreductase
Q27PX2
-
lipoxygenase 2
-
-
lipoxygenase-2
P38418
-
lipoxygenase-3
Q9LNR3
-
lipoxygenase-4
Q9FNX8
-
lipoxygenase-6
Q9CAG3
-
LOX
B5SXD0
-
LOX
Fusarium oxysporum 4287
-
-
-
LOX
Ipomoea nil Choisy
-
-
-
LOX
Pseudomonas aeruginosa BBE
-
-
-
LOX-2
-
-
LOX1
Q27PX2
-
LOX2
Q6X5R6
-
LOX2:Hv:1
P93184
-
LOX3
Q6X5R5
-
Oep1LOX2
-
-
Oep2LOX2
-
-
SBLO-1
-
-
soybean lipoxygenase-1
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-60-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strains NRRL 3357, TSHB3.1C and TSHB3.5C
UniProt
Manually annotated by BRENDA team
f. sp. lycopersici
-
-
Manually annotated by BRENDA team
Fusarium oxysporum 4287
f. sp. lycopersici
-
-
Manually annotated by BRENDA team
cv. Salome
SwissProt
Manually annotated by BRENDA team
cv. Sun Smile
-
-
Manually annotated by BRENDA team
Ipomoea nil Choisy
cv. Sun Smile
-
-
Manually annotated by BRENDA team
PCC73102
SwissProt
Manually annotated by BRENDA team
Nostoc punctiforme PCC73102
PCC73102
SwissProt
Manually annotated by BRENDA team
; cv. Picual
-
-
Manually annotated by BRENDA team
cv. Aichiasahi
Uniprot
Manually annotated by BRENDA team
Pseudomonas aeruginosa BBE
-
-
-
Manually annotated by BRENDA team
gene tomloxD
-
-
Manually annotated by BRENDA team
L. cv Desiree
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
B5SXD0
deletion of lox greatly diminishes density-dependent development of both sclerotia and conidia, resulting in an overall increase in the number of sclerotia and a decrease in the number of conidia at high cell densities. Lox mutants show decreased linoleic acid LOX activity
malfunction
-, Q6X5R5, Q6X5R6
reduced LOX2 expression decreases the release of green leaf volatiles but does not impair jasmonic acid and jasmonic acid-Ile accumulation
physiological function
B6D1W5
9/13-LOX is associated with the ripening and senescence processes
physiological function
-
expression of 15-LO-1 significantly decreases cell proliferation and increases apoptosis. Reduces adhesion to fibronectin, anchorage-independent growth on soft agar, cellular motility and ability to heal a scratch wound, and migratory and invasive capacity across Matrigel. 15-LO-1 expression reduces the expression of metastasis associated protein-1, a part of the nucleosome remodeling and histone deacetylase silencing complex
physiological function
-
major involvement of the Oep2LOX2 gene in the biosynthesis of virgin olive oil aroma compounds
physiological function
P38418, Q9CAG3, Q9FNX8, Q9LNR3
LOX-2 is a 13S-lipoxygenases, it has no dual positional specificity; LOX-3 is a 13S-lipoxygenases, it has no dual positional specificity; LOX-4 is a 13S-lipoxygenases, it has no dual positional specificity; LOX-6 is a 13S-lipoxygenases, it has no dual positional specificity
physiological function
Q27PX2
LOX1 is a non-conventional LOX with 13- or dual position-specific LOX activity. LOX1 is involved in the synthesis of jasmonic acid, colneleic acid, and (Z)-3-hexenal. The LOX1 product is involved in tolerance of the rice plant to wounding and brown planthopper Nilaparvata lugens attack
physiological function
-
involvement of Cd-induced LOX activity in the premature differentiation of the barley root tip during Cd stress
physiological function
-
plant lipoxygenases catalyse the oxygenation of polyunsaturated fatty acids, linoleic and alpha-linolenic acid and are involved in processes such as stress responses and development
physiological function
-
the enzyme is involved in endogenous JA synthesis and tolerance to biotic and abiotic stress
metabolism
-
depending on the regiospecificity of the enzyme, the incorporation of molecular oxygen leads to formation of 9- or 13-fatty acid hydroperoxides, which are used by LOX itself as well as by members of at least six different enzyme families to form a series of biologically active molecules, collectively called oxylipins
additional information
-
non-heme iron lipoxygenase oxidizes C18-polyunsaturated fatty acids to 13S-hydroperoxy derivatives by an antarafacial reaction mechanism where the bis-allylic hydrogen abstraction is the rate-limiting step
additional information
Fusarium oxysporum 4287
-
non-heme iron lipoxygenase oxidizes C18-polyunsaturated fatty acids to 13S-hydroperoxy derivatives by an antarafacial reaction mechanism where the bis-allylic hydrogen abstraction is the rate-limiting step
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(15S)-hydroperoxyeicosatetraenoic acid + O2
(8S,15S)-dihydroperoxyeicosatetraenoic acid + (5S,15S)-dihydroperoxyeicosatetraenoic acid
show the reaction diagram
-
-
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetra-5,8,11,14-enoic acid + O2
?
show the reaction diagram
Fusarium oxysporum, Fusarium oxysporum 4287
-
-
-
-
?
(7Z,10Z,13Z)-hexadecatrienoic acid + O2
?
show the reaction diagram
-
lipoxygenase 2 produces 7- (21.5%), 8- (12.3%), 10- (12.9%), 11- (14.5%), 13- (14%), and 14- (19.6%) hydroperoxides of 16:3, as well as a significant amount of bis-allylic 9-hydroperoxide (5.2%)
-
-
?
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
?
show the reaction diagram
Fusarium oxysporum, Fusarium oxysporum 4287
-
-
-
-
?
(9Z,12Z,15Z)-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
Fusarium oxysporum, Fusarium oxysporum 4287
-
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
-
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
-
-
-
-
?
(9Z,9Z,12Z)-octadeca-6,9,12-trienoic acid + O2
?
show the reaction diagram
-
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
-
-
-
-
?
alpha-linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Ipomoea nil, Ipomoea nil Choisy
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
show the reaction diagram
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
show the reaction diagram
B2IZG6
alpha-linolenate is the preferred substrate
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
show the reaction diagram
-
Lox2 and Lox3 are more active against linolenate compared to linoleate
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
show the reaction diagram
Nostoc punctiforme PCC73102
B2IZG6
alpha-linolenate is the preferred substrate
-
-
?
alpha-linolenate + O2
(9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
show the reaction diagram
-
isoenzyme Oep1LOX2 and Oep2LOX2 both produce primarily 13-hydroperoxides from linoleic acid and linolenic acid. Linolenic acid is the preferred substrate for both isoenzymes (Vmax/KM is about 10fold higher for linolenic acid)
-
-
?
alpha-linolenic acid + O2
?
show the reaction diagram
-
-
-
-
?
gamma-linolenate + O2
(6Z,9Z,11E,13S)-13-hydroperoxy-6,9,11-octadecatrienoate
show the reaction diagram
Nostoc punctiforme, Nostoc punctiforme PCC73102
B2IZG6
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Q27PX2
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-, Q6X5R5, Q6X5R6
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
primary product
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
lipoxygenase 2 specifically oxidizes linoleate into 13-hydroperoxide
-
-
?
linoleate + O2
(9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
isoenzyme Oep1LOX2 and Oep2LOX2 both produce primarily 13-hydroperoxides from linoleic acid and linolenic acid. Linolenic acid is the preferred substrate for both isoenzymes (Vmax/KM is about 10fold higher for linolenic acid)
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
P93184
-
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-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
-
the ratio of (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is 87:13 for the enzyme from cucumber cotyledons, and 84:16 for the recombinant enzyme. A linoleate 9-LOX preferentially oxygenates free fatty acids whereas a linoleate 13-LOX is capable of oxygenating triolein to significantly higher degrees in all positions of the triacylglycerol. For 9-LOXs, the carboxylate anion of the substrate may be the binding or recognition site within the catalytic pocket of the enzyme, whereas in the case of 13-LOXs the unpolar hydrophobic tail of the fatty acid may be orientated towards the catalytic pocket of the enzyme. This may explain why unpolar substrates, such as trilinolein, are preferred substrates for linoleate 13-LOXs
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
B2IZG6
-
the ratio of (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate to (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate is higher than 80:20 at all pH values tested
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
P38419
-
the ratio of the 13-hydroperoxy to 9-hydroperoxy fatty acid reaction is 98:2. The R/S stereoconfiguration of the product is not determined
-
?
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)
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
-
Lox2 and Lox3 are more active against linolenate compared to linoleate
the R/S stereoconfiguration of the product is not determined
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
P38418, Q9CAG3, Q9FNX8, Q9LNR3
the enzyme oxygenates linolenic acid more effectively than linoleic acid
the enzyme forms exclusively (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
show the reaction diagram
Nostoc punctiforme PCC73102
B2IZG6
-
the ratio of (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate to (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate is higher than 80:20 at all pH values tested
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
product identification by HPLC of recombinant extracellular enzyme, overview
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Fusarium oxysporum 4287
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Pseudomonas aeruginosa BBE
-
-
-, product identification by HPLC of recombinant extracellular enzyme, overview
-
?
linoleic acid + O2
?
show the reaction diagram
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
B5SXD0
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
B7FDE5, -
-
at pH-values higher than 7.5 the enzyme constitutes a linoleate 13-LOX whereas at lower pH, 9-H(P)ODE is the major reaction product. Glutamine 599 plays a role in pH-dependence of the reaction specificity
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
B6D1W5
-
the recombinant enzyme shows a dual positional specificity, as it forms both 9- and 13-hydroperoxy octadecadienoic acid in a ratio 2:1
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
-
preferred substrate
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
show the reaction diagram
-
4-nitroso-N,N-dimethylaniline bleaching in the course of linoleate hydroperoxidation by soybean LOX-1
-
-
?
linoleic acid + O2
13(S)-hydroxyoctadecadienoic acid
show the reaction diagram
-
-
-
-
?
linolenate + O2
?
show the reaction diagram
P38418, Q9CAG3, Q9FNX8, Q9LNR3
the enzyme oxygenates linolenic acid more effectively than linoleic acid
the product is not determined
-
?
linolenic acid + O2
?
show the reaction diagram
-
-
-
-
?
linolenic acid + O2
?
show the reaction diagram
B6D1W5
-
-
-
?
linolenic acid + O2
?
show the reaction diagram
P38418, Q9CAG3, Q9FNX8, Q9LNR3
LOX-2 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
show the reaction diagram
P38418, Q9CAG3, Q9FNX8, Q9LNR3
LOX-3 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
show the reaction diagram
P38418, Q9CAG3, Q9FNX8, Q9LNR3
LOX-4 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
show the reaction diagram
P38418, Q9CAG3, Q9FNX8, Q9LNR3
LOX-6 displays a selective oxygenation of linolenic acid
-
-
?
N-linolenoylethanolamide + O2
?
show the reaction diagram
-
-
-
-
?
N-linoleoylethanolamide + O2
?
show the reaction diagram
-
-
-
-
?
linoleyltrimethylammonium ion + O2
13-hydroperoxy-(9Z,11E,13S)-octadecadienyltrimethylammonium ion
show the reaction diagram
-
-
primarily
-
?
additional information
?
-
P38418, Q9CAG3, Q9FNX8, Q9LNR3
arachidonic acid is a poor substrate
-
-
-
additional information
?
-
-
oxygenation of triolein by lipid body LOX leads to a trihydroperoxy derivative
-
-
-
additional information
?
-
P93184
the enzyme also converts arachidonate into (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate, S/R ratio is 92:8
-
-
-
additional information
?
-
B2IZG6
the enzyme also converts arachidonate to its (15S)-hydroperoxide. The enzyme shows no substrate preference
-
-
-
additional information
?
-
P38419
the enzyme also converts linolenate into the 13-hydroperoxyy fatty acid
-
-
-
additional information
?
-
-
LOX-1 barely reacts with (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate alone
-
-
-
additional information
?
-
-
under anaerobic conditions, LOX-1 shows LTA synthase activity with (15S)-hydroperoxyeicosatetraenoic acid as substrate giving either 14,15-leukotriene A4 or 5,15-dihydroxyeicosatetraenoic acid
-
-
-
additional information
?
-
-
LOXs catalyze the regio- and stereospecific dioxygenation of polyunsaturated fatty acids with a (1Z,4Z)-pentadiene structure
-
-
-
additional information
?
-
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
-
additional information
?
-
-
identification of products, by biotransformation and mass spectrometry, determination of the stereochemistry of the major product, overview
-
-
-
additional information
?
-
Fusarium oxysporum 4287
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
-
additional information
?
-
Nostoc punctiforme PCC73102
B2IZG6
the enzyme also converts arachidonate to its (15S)-hydroperoxide. The enzyme shows no substrate preference
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
-
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
show the reaction diagram
-
-
-
-
?
alpha-linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Ipomoea nil, Ipomoea nil Choisy
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-, Q6X5R5, Q6X5R6
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
lipoxygenase 2 specifically oxidizes linoleate into 13-hydroperoxide
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Fusarium oxysporum 4287
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
show the reaction diagram
Pseudomonas aeruginosa BBE
-
-
-
-
?
additional information
?
-
-
LOXs catalyze the regio- and stereospecific dioxygenation of polyunsaturated fatty acids with a (1Z,4Z)-pentadiene structure
-
-
-
additional information
?
-
Fusarium oxysporum, Fusarium oxysporum 4287
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cadmium
-
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 21C increases with increasing temperatures
Fe
B5SXD0
the iron atom in LOX is bound by four ligands, three of which are histidine residues
Fe
-
LOX-1 exists in two oxidation states, Fe(II) and Fe(III)
Fe
-
the ferric enzyme is responsible for the catalytic activity
Fe2+
-
weakly active site-bound, required for catalysis, non-heme iron lipoxygenase
Fe3+
-
the allyloxy group of compounds is oriented towards the Fe(3+)-OH moiety in the active site of the enzyme
Fe3+
-
the carbonyl group of inhibitors is oriented towards the Fe(III)-OH moiety in the active site of the enzyme
Fe3+
-
among the conserved amino acids in sequences of both isozymes are three His, one Asn, and one Ile residue, which are essential for the binding of the atom of iron in the active site of the LOXs enzymes
Iron
-
nonheme, iron-containing dioxygenase
additional information
-
specifically binds iron but not manganese
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-(4-methoxyphenyl)-2-butanone
-
-
1-(4-methoxyphenyl)acetone
-
-
1-methoxy-4-(2-ethylallyl)benzene
-
-
1-methoxy-4-(2-methylallyl)benzene
-
-
11-thialinoleic acid
-
is a competitive inhibitor with respect to linoleic acid and a noncompetitive inhibitor with respect to arachidonic acid
14-thialinoleic acid
-
is a competitive inhibitor with respect to linoleic acid
2',4,6-trimethoxy-aurone
-
-
2'-hydroxy-2,4',6'-trimethoxy-chalcone
-
exhibits 20% inhibition
2'-hydroxy-2-methoxy-chalcone
-
-
2'-hydroxy-3,4,4',6'-tetra(methoxymethoxy)-chalcone
-
exhibits 14.1% inhibition
2'-hydroxy-3,4-dimethoxy-chalcone
-
-
2'-hydroxy-3-methoxy-chalcone
-
exhibits 36.4% inhibition
2'-hydroxy-4-chloro-4', 6'-dimethoxy-chalcone
-
-
2'-hydroxy-4-chloro-chalcone
-
-
2'-hydroxy-4-methyl-4',6'-dimethoxy-chalcone
-
-
2'-hydroxy-4-methyl-chalcone
-
-
2'-methoxy-aurone
-
exhibits 39.9% inhibition
2-(3,4-dihydroxybenzoyl)-2,4,6-trihydroxybenzofuran-3(2H)-one
-
quercetin is slowly oxidized by hydroperoxides to a rather stable intermediate, 2-(3,4-dihydroxybenzoyl)-2,4,6-trihydroxybenzofuran-3(2H)-one, which still inhibits the enzymatic oxidation, probably as a chelator
-
2-(3-(hydroxy(phenyl)methyl)phenyl)-N-phenethylpropanamide
-
-
-
2-(3-(hydroxy(phenyl)methyl)phenyl)propanoic acid
-
-
-
2-(3-benzoylphenyl)-N-(cyclohexanemethyl)propanamide
-
-
-
2-(3-benzoylphenyl)-N-cyclohexylpropanamide
-
-
-
2-(3-benzoylphenyl)-N-cyclopentylpropanamide
-
-
-
2-(3-benzoylphenyl)-N-phenethylpropanamide
-
-
-
2-(3-benzylphenyl)-N,N-bis(2-hydroxyethyl)propanamide
-
-
-
2-(3-benzylphenyl)-N-(2-hydroxyethyl)propanamide
-
-
-
2-(3-benzylphenyl)-N-(3-hydroxypropyl)propanamide
-
-
-
2-(3-benzylphenyl)-N-(cyclohexanemethyl)propanamide
-
-
-
2-(3-benzylphenyl)-N-cyclohexylpropanamide
-
-
-
2-(3-benzylphenyl)-N-cyclopentylpropanamide
-
-
-
2-(3-benzylphenyl)-N-ethoxypropanamide
-
-
-
2-(3-benzylphenyl)-N-methoxypropanamide
-
12% and 27.5% inhibition at 0.1 and 0.5 mM, respectively
-
2-(3-benzylphenyl)-N-phenethylpropanamide
-
-
-
2-(3-benzylphenyl)propanamide
-
-
-
2-(3-benzylphenyl)propanoic acid
-
-
-
2-dodecyl-6-hydroxybenzoic acid
-
C12:0, competitive inhibitor
2-hydroxy-6-[(8E)-pentadec-8-en-1-yl]benzoic acid
-
C15:1, E-isomer, competitive inhibitor
3'-methoxy-aurone
-
exhibits 34.9% inhibition
4'-chloro-4, 6-dimethoxy-aurone
-
-
4'-chloro-aurone
-
exhibits 26.4% inhibition
4'-methoxy-aurone
-
-
4'-methyl-aurone
-
exhibits 32.4% inhibition
4,4',6-trimethoxy-aurone
-
best LOX inhibitory activity
4-(allyloxy)phenyl benzoate
-
-
4-allylphenyl benzoate
-
-
4-Methoxyphenylacetic acid
-
-
6-(2'-ethylheptyl)salicylic acid
-
-
6-(4',8'-dimethylnonyl) salicylic acid
-
-
6-pentadecanylsalicylic acid
-
competitive inhibitor, dose-dependent inhibitory effect
6-[2'-(2'',4'',5''-trihydroxyphenyl)etyl]salicylic acid
-
inhibits lipoxygenase-catalyzed oxidation of linoleic acid, but to a lesser extent compared to 6-pentadecanylsalicylic acid
6-[2'-(2'',4''-dihydroxyphenyl)ethyl]salicylic acid
-
inhibits lipoxygenase-catalyzed oxidation of linoleic acid, but to a lesser extent compared to 6-pentadecanylsalicylic acid
6-[2'-(2'',5''-dihydroxyphenyl)ethyl]salicylic acid
-
inhibits lipoxygenase-catalyzed oxidation of linoleic acid, but to a lesser extent compared to 6-pentadecanylsalicylic acid
6-[2'-(3'',4''-dihydroxyphenyl)ethyl]salicylic acid
-
inhibits lipoxygenase-catalyzed oxidation of linoleic acid, but to a lesser extent compared to 6-pentadecanylsalicylic acid
6-[8(Z),11(Z),14-pentadecatrienyl]salicylic acid
-
from Anacardium occidentale
6-[8(Z),11(Z)-pentadecadienyl]salicylic acid
-
from Anacardium occidentale
6-[8(Z)-pentadecenyl]salicylic acid
-
from Anacardium occidentale
alpha-tocopherol
-
competitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
apigenin
-
uncompetitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
beta-carotene
-
-
butyl 2-(4-methoxyphenyl)acetate
-
-
caffeic acid
-
-
catechin
-
competitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
Cu2+
-
inhibits Oep2LOX2 by 49%
cyanidin
-
from Aronia melanocarpa concentrate, inhibits in a concentration-dependent manner
cyanidin 3-O-arabinoside
-
from Aronia melanocarpa concentrate, inhibits in a concentration-dependent manner
cyanidin 3-O-galactoside
-
from Aronia melanocarpa concentrate, inhibits in a concentration-dependent manner
cyanidin 3-O-glucoside
-
from Aronia melanocarpa concentrate, inhibits in a concentration-dependent manner
cyclohexyl 2-(4-methoxyphenyl)acetate
-
-
cyclopentyl 2-(4-methoxyphenyl)acetate
-
-
delphinidin
-
from Vaccinium myrtillus berries, inhibits in a concentration-dependent manner
delphinidin 3-O-arabinoside
-
from Vaccinium myrtillus berries, inhibits in a concentration-dependent manner
delphinidin 3-O-galactoside
-
from Vaccinium myrtillus berries, most effective inhibitor, uncompetitive type, inhibits in a concentration-dependent manner
delphinidin 3-O-glucoside
-
from Vaccinium myrtillus berries, most effective inhibitor, uncompetitive type, inhibits in a concentration-dependent manner
esteragol
-
-
estragol
-
-
ethyl 2-(4-methoxyphenyl)acetate
-
-
eugenyl benzoate
-
-
Fe3+
-
slight inactivation
-
ferulic acid
-
noncompetitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
Gallic acid
-
competitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
glutathione
-
-
hexyl 2-(4-methoxyphenyl)acetate
-
-
Hg2+
-
inhibits Oep1LOX2 by 60% and totally inactivates Oep2LOX2
isobutyl 2-(4-methoxyphenyl)acetate
-
-
isopropyl 2-(4-methoxyphenyl)acetate
-
-
kaempferol
-
-
Ketoprofen
-
-
L-ascorbic acid
-
noncompetitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
lauric acid
-
-
lauroylethanolamide
-
-
-
N-benzhydryl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
-
N-benzhydryl-2-(3-benzoylphenyl)propanamide
-
-
-
N-benzhydryl-2-(3-benzylphenyl)propanamide
-
-
-
N-benzyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
-
N-benzyl-2-(3-benzoylphenyl)propanamide
-
-
-
N-benzyl-2-(3-benzylphenyl)propanamide
-
-
-
N-benzyloxy-2-(3-benzylphenyl)propanamide
-
-
-
N-cyclohexanemethyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
-
N-cyclohexyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
-
N-cyclopentyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
-
N-hydroxy-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
-
n-propyl gallate
-
causes a strong inhibition of the LOX-catalyzed enzymatic reaction
N1-(4-(allyloxy) phenyl)-1-admantancarboxamide
-
best inhibitor
N1-(4-(allyloxy) phenyl)-1-cyclobutanecarboxamide
-
-
N1-(4-(allyloxy) phenyl)-1-cyclohexanecarboxamide
-
-
N1-(4-(allyloxy) phenyl)-1-cyclopantanecarboxamide
-
-
N1-(4-(allyloxy) phenyl)-1-cyclopropanecarboxamide
-
-
N1-(4-(allyloxy) phenyl)-2-methylpropanamide
-
-
N1-(4-(allyloxy) phenyl)-3-chlorobenzamide
-
-
N1-(4-(allyloxy) phenyl)-3-fluorobenzamide
-
-
N1-(4-(allyloxy) phenyl)-3-methoxybenzamide
-
-
N1-(4-(allyloxy) phenyl)-3-methylbenzamide
-
-
N1-(4-(allyloxy) phenyl)-4-chlorobenzamide
-
-
N1-(4-(allyloxy) phenyl)-4-fluorobenzamide
-
-
N1-(4-(allyloxy) phenyl)-4-methoxybenzamide
-
-
N1-(4-(allyloxy) phenyl)-4-methylbenzamide
-
-
N1-(4-(allyloxy) phenyl)benzamide
-
-
nordihydroguaiaretic acid
B6D1W5
is a noncompetitive inhibitor
nordihydroguaiaretic acid
-
-
pentyl 2-(4-methoxyphenyl)acetate
-
long chain and lipophile 4-methoxyphenylacetic acid ester, behaves as the best SLO inhibitor
peonidin
-
from Vaccinium macrocarpon juice, inhibits in a concentration-dependent manner
peonidin 3-O-arabinoside
-
from Vaccinium macrocarpon juice, inhibits in a concentration-dependent manner
peonidin 3-O-galactoside
-
from Vaccinium macrocarpon juice, inhibits in a concentration-dependent manner
peonidin 3-O-glucoside
-
from Vaccinium macrocarpon juice, inhibits in a concentration-dependent manner
Phenidone
-
inhibits the LOX-dependent defence response of the plant, whereby this inhibition can influence the behaviour of members of the associated insect community. Plants treated with phenidone are less attractive to Cotesia glomerata parasitoids than controls. Herbivores Pieris rapae and Pieris brassicae are less sensitive to changes in plant metabolic profiles induced by caterpillar feeding and LOX inhibition respectively than their natural enemy Cotesia glomerata. Preference of Plutella xylostella for Pieris rapae-infested plants over uninfested plants is LOX dependent, since phenidone treatment of uninfested and infested plants eliminates the preference. The inhibitor reduces the accumulation of internal signalling compounds in the octadecanoid pathway of the plant downstream of the step catalysed by LOX, i.e. 12-oxo-phytodienoic acid and jasmonic acid
propyl 2-(4-methoxyphenyl)acetate
-
-
propyl gallate
B6D1W5
is a competitive inhibitor
quercetin
-
noncompetitive inhibition by initially reducing the ferric form of the enzyme to an inactive ferrous form
resveratrol
-
uncompetitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
sec-butyl 2-(4-methoxyphenyl)acetate
-
-
tert-butyl 2-(4-methoxyphenyl)acetate
-
-
Trolox
-
noncompetitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction. At physiological pH 7.0 the LOX/4-nitroso-N,N-dimethylaniline assay is more sensitive to trolox inhibition
methyleugenol
-
-
additional information
-
4-allyloxyaniline amides designed as inhibitors on the basis of eugenol and esteragol structures. Compounds are docked in SLO active site and fixed by hydrogen bonding with two conserved His513 and Gln716. Molecular volume of the amide moiety is a major factor in inhibitory potency variation of the synthetic amides, where the hydrogen bonding of the amide group can involve in the activity of the inhibitors
-
additional information
-
4-methoxyphenylacetic acid esters designed as inhibitors on the basis of eugenol and esteragol structures are docked in SLO active site and show that carbonyl group of compounds is oriented toward the FeIII-OH moiety in the active site of enzyme and fixed by hydrogen bonding with hydroxyl group. Lipophilic interaction of ligand-enzyme is in charge of inhibiting the enzyme activity. Is not inhibited by 6-methoxy-2-methylene-1,2,3,4-tetrahydronaphthalene
-
additional information
-
chalcones exhibit superior LOX inhibitory activity than aurones. 2'-hydroxy-4-methoxy-chalcone, 2'-hydroxy-3,4,4',6'-tetramethoxy-chalcone, 2'-hydroxy-4,4',6'-trimethoxy-chalcone, 2',3,4,4',6'-pentahydroxy-chalcone, aureusidin, 4,6-dimethoxy-4'-methyl-aurone and 3',4,4',6-tetra(methoxymethyl)-aurone have no or very low LOX inhibitory activity
-
additional information
-
LOX/4-nitroso-N,N-dimethylaniline reaction is not inhibited by inulin
-
additional information
-
is not inhibited by malvidin 3-O-glucoside from Vaccinium myrtillus berries
-
additional information
-
presence of inhibitor does not change the regioselectivity of lipoxygenase-1
-
additional information
-
3,4-dihydro-7-hydroxycadalin, 7-hydroxycadalin, 3-hydroxyphenylacetic acid, 4-hydroxy-3-methoxyphenylacetic acid, and 3,4-dihydroxyphenylacetic acid do not inhibit the soybean lipoxygenase-1 catalyzed lipid peroxidation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
13-hydroperoxy-linoleic acid
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00337
-
(5Z,8Z,11Z,14Z)-eicosatetra-5,8,11,14-enoic acid
-
pH 8.0, 22C
-
0.00689
-
(9Z,12Z)-octadeca-9,12-dienoic acid
-
pH 8.0, 22C
0.0316
-
(9Z,12Z,15Z)-9,12,15-octadecatrienoic acid
-
pH 8.0, 22C
-
0.0348
-
(9Z,9Z,12Z)-octadeca-6,9,12-trienoic acid
-
pH 8.0, 22C
-
0.028
-
alpha-linolenate
-
pH 6.5, 20C, isoenzyme Oep1LOX2
0.032
-
alpha-linolenate
-
in 0.1 M borate (pH 9.0), temperature not specified in the publication
0.14
-
alpha-linolenate
-
pH 6.5, 20C, isoenzyme Oep2LOX2
0.0146
-
linoleate
-
pH 6.5, 20C, isoenzyme Oep1LOX2
0.021
-
linoleate
-
in 0.1 M borate (pH 9.0), temperature not specified in the publication
0.0489
-
linoleate
-
pH 7.5, 25C, recombinant enzyme
0.13
-
linoleate
-
pH 6.5, 20C, isoenzyme Oep2LOX2
0.0117
-
linoleic acid
-
in the presence of 2-hydroxy-6-[(8E)-pentadec-8-en-1-yl]benzoic acid
0.01191
-
linoleic acid
-
-
0.0131
-
linoleic acid
-
in the presence of 6-pentadecanylsalicylic acid
0.0132
-
linoleic acid
-
in the presence of 2-dodecyl-6-hydroxybenzoic acid
0.01459
-
linoleic acid
-
isoform Oep1LOX2
0.028
-
linoleic acid
-
-
0.043
-
linoleic acid
-
55fold purified enzyme, at pH 8.8, isoform 2
0.08
-
linoleic acid
-
48fold purified enzyme, at pH 8.8, isoform 1
0.1297
-
linoleic acid
-
isoform Oep2LOX2
0.1749
-
linoleic acid
B6D1W5
pH 6.0, 25C
0.028
-
linolenic acid
-
isoform Oep1LOX2
0.1389
-
linolenic acid
-
isoform Oep2LOX2
0.015
-
N-linolenoylethanolamide
-
in 0.1 M borate (pH 9.0), temperature not specified in the publication
-
0.027
-
N-linoleoylethanolamide
-
in 0.1 M borate (pH 9.0), temperature not specified in the publication
-
0.3437
-
linolenic acid
B6D1W5
pH 6.0, 25C
additional information
-
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.71
-
(5Z,8Z,11Z,14Z)-eicosatetra-5,8,11,14-enoic acid
-
pH 8.0, 22C
-
2.611
-
(9Z,12Z)-octadeca-9,12-dienoic acid
-
pH 8.0, 22C
1.566
-
(9Z,12Z,15Z)-9,12,15-octadecatrienoic acid
-
pH 8.0, 22C
-
18.58
-
(9Z,9Z,12Z)-octadeca-6,9,12-trienoic acid
-
pH 8.0, 22C
-
48.16
-
linoleic acid
B6D1W5
pH 6.0, 25C
64
-
linoleic acid
-
-
47.78
-
linolenic acid
B6D1W5
pH 6.0, 25C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
25
-
linoleic acid
-
-
12640
280
-
linoleic acid
B6D1W5
-
12640
140
-
linolenic acid
B6D1W5
-
12642
additional information
-
additional information
-
linolenic acid is the preferred substrate for both isoenzymes (Vmax/KM is about 10fold higher for linolenic acid)
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.022
-
11-thialinoleic acid
-
-
0.035
-
14-thialinoleic acid
-
-
0.0096
-
2-dodecyl-6-hydroxybenzoic acid
-
pH 9.0
0.0028
-
2-hydroxy-6-[(8E)-pentadec-8-en-1-yl]benzoic acid
-
pH 9.0
0.0064
-
6-pentadecanylsalicylic acid
-
pH 9.0
1.1
-
alpha-tocopherol
-
-
3.4
-
apigenin
-
-
13.6
-
catechin
-
-
10.7
-
ferulic acid
-
-
6.7
-
Gallic acid
-
-
14
-
L-ascorbic acid
-
-
0.0084
-
lauric acid
-
using N-linoleoylethanolamide as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
0.0121
-
lauric acid
-
using linoleate as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
0.0146
-
lauric acid
-
using N-linolenoylethanolamide as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
0.015
-
lauric acid
-
using alpha-linolenate as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
0.0005
-
lauroylethanolamide
-
using linoleate as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
-
0.0006
-
lauroylethanolamide
-
using N-linoleoylethanolamide as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
-
0.0007
-
lauroylethanolamide
-
using N-linolenoylethanolamide as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
-
0.0009
-
lauroylethanolamide
-
using alpha-linolenate as substrate, in 0.1 M borate (pH 9.0), temperature not specified in the publication
-
0.00409
-
nordihydroguaiaretic acid
B6D1W5
pH 6.0, 25C
0.00188
-
propyl gallate
B6D1W5
pH 6.0, 25C
1.7
-
resveratrol
-
-
7
-
Trolox
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.033
-
1-(4-methoxyphenyl)-2-butanone
-
pH 9.0, 20C
0.043
-
1-(4-methoxyphenyl)acetone
-
pH 9.0, 20C
0.145
-
1-methoxy-4-(2-ethylallyl)benzene
-
pH 9.0, 20C
0.137
-
1-methoxy-4-(2-methylallyl)benzene
-
pH 9.0, 20C
0.1
-
2',4,6-trimethoxy-aurone
-
at pH 9.0
0.1
-
2'-hydroxy-2-methoxy-chalcone
-
at pH 9.0
0.0675
-
2'-hydroxy-3,4-dimethoxy-chalcone
-
at pH 9.0
0.082
-
2'-hydroxy-4-chloro-4', 6'-dimethoxy-chalcone
-
at pH 9.0
0.056
-
2'-hydroxy-4-chloro-chalcone
-
at pH 9.0
0.053
-
2'-hydroxy-4-methyl-4',6'-dimethoxy-chalcone
-
at pH 9.0
0.0525
-
2'-hydroxy-4-methyl-chalcone
-
at pH 9.0
0.12
-
2-(3-(hydroxy(phenyl)methyl)phenyl)-N-phenethylpropanamide
-
25C, pH not specified in the publication
-
0.13
-
2-(3-(hydroxy(phenyl)methyl)phenyl)propanoic acid
-
25C, pH not specified in the publication
-
0.053
-
2-(3-benzoylphenyl)-N-(cyclohexanemethyl)propanamide
-
25C, pH not specified in the publication
-
0.12
-
2-(3-benzoylphenyl)-N-cyclohexylpropanamide
-
25C, pH not specified in the publication
-
0.0615
-
2-(3-benzoylphenyl)-N-cyclopentylpropanamide
-
25C, pH not specified in the publication
-
0.065
-
2-(3-benzoylphenyl)-N-phenethylpropanamide
-
25C, pH not specified in the publication
-
0.4
-
2-(3-benzylphenyl)-N,N-bis(2-hydroxyethyl)propanamide
-
25C, pH not specified in the publication
-
0.27
-
2-(3-benzylphenyl)-N-(2-hydroxyethyl)propanamide
-
25C, pH not specified in the publication
-
0.28
-
2-(3-benzylphenyl)-N-(3-hydroxypropyl)propanamide
-
25C, pH not specified in the publication
-
0.08
-
2-(3-benzylphenyl)-N-(cyclohexanemethyl)propanamide
-
25C, pH not specified in the publication
-
0.0375
-
2-(3-benzylphenyl)-N-cyclohexylpropanamide
-
25C, pH not specified in the publication
-
0.082
-
2-(3-benzylphenyl)-N-cyclopentylpropanamide
-
25C, pH not specified in the publication
-
0.385
-
2-(3-benzylphenyl)-N-ethoxypropanamide
-
25C, pH not specified in the publication
-
0.043
-
2-(3-benzylphenyl)-N-phenethylpropanamide
-
25C, pH not specified in the publication
-
0.325
-
2-(3-benzylphenyl)propanamide
-
25C, pH not specified in the publication
-
0.415
-
2-(3-benzylphenyl)propanoic acid
-
25C, pH not specified in the publication
-
0.00207
-
2-dodecyl-6-hydroxybenzoic acid
-
pH 9.0
0.0068
-
2-hydroxy-6-[(8E)-pentadec-8-en-1-yl]benzoic acid
-
pH 9.0
0.07
-
4'-methoxy-aurone
-
at pH 9.0
0.05
-
4,4',6-trimethoxy-aurone
-
at pH 9.0
0.0062
-
4-(allyloxy)phenyl benzoate
-
pH 9.0, 20C
0.0067
-
4-allylphenyl benzoate
-
pH 9.0, 20C
0.0562
-
4-Methoxyphenylacetic acid
-
pH 9.0, 20C
0.0188
-
6-(2'-ethylheptyl)salicylic acid
-
pH 9.0
0.0105
-
6-(4',8'-dimethylnonyl) salicylic acid
-
pH 9.0
0.0143
-
6-pentadecanylsalicylic acid
-
pH 9.0
0.4
-
6-[2'-(2'',5''-dihydroxyphenyl)ethyl]salicylic acid
-
pH 9.0
0.0078
-
beta-carotene
-
-
0.0038
-
butyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.6
-
caffeic acid
-
at pH 9.0
0.6
-
caffeic acid
-
25C, pH not specified in the publication
0.58
-
cyanidin
-
-
1.24
-
cyanidin 3-O-arabinoside
-
-
0.18
-
cyanidin 3-O-galactoside
-
-
0.25
-
cyanidin 3-O-glucoside
-
-
0.064
-
cyclohexyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.0565
-
cyclopentyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.27
-
delphinidin
-
-
0.49
-
delphinidin 3-O-arabinoside
-
-
0.00046
-
delphinidin 3-O-galactoside
-
-
0.00043
-
delphinidin 3-O-glucoside
-
-
0.0641
-
esteragol
-
pH 9.0, 20C
0.0641
-
estragol
-
pH 9.0, 20C
0.032
-
ethyl 2-(4-methoxyphenyl)acetate
-
-
0.0382
-
Eugenol
-
pH 9.0, 20C
0.007
-
eugenyl benzoate
-
pH 9.0, 20C
0.0197
-
glutathione
-
-
0.035
-
hexyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.0881
-
isobutyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.0344
-
isopropyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.13
-
Ketoprofen
-
25C, pH not specified in the publication
0.0961
-
methyleugenol
-
pH 9.0, 20C
0.0205
-
N-benzhydryl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
25C, pH not specified in the publication
-
0.0645
-
N-benzhydryl-2-(3-benzoylphenyl)propanamide
-
25C, pH not specified in the publication
-
0.05
-
N-benzhydryl-2-(3-benzylphenyl)propanamide
-
25C, pH not specified in the publication
-
0.2
-
N-benzyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
25C, pH not specified in the publication
-
0.0875
-
N-benzyl-2-(3-benzoylphenyl)propanamide
-
25C, pH not specified in the publication
-
0.0745
-
N-benzyl-2-(3-benzylphenyl)propanamide
-
25C, pH not specified in the publication
-
0.1
-
N-benzyloxy-2-(3-benzylphenyl)propanamide
-
25C, pH not specified in the publication
-
0.295
-
N-cyclohexanemethyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
25C, pH not specified in the publication
-
0.425
-
N-cyclohexyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
25C, pH not specified in the publication
-
0.23
-
N-cyclopentyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
25C, pH not specified in the publication
-
0.2
-
N-hydroxy-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
25C, pH not specified in the publication
-
0.00067
-
N1-(4-(allyloxy) phenyl)-1-admantancarboxamide
-
pH 9.0, 20C
0.0022
-
N1-(4-(allyloxy) phenyl)-1-cyclobutanecarboxamide
-
pH 9.0, 20C
0.0064
-
N1-(4-(allyloxy) phenyl)-1-cyclohexanecarboxamide
-
pH 9.0, 20C
0.0041
-
N1-(4-(allyloxy) phenyl)-1-cyclopantanecarboxamide
-
pH 9.0, 20C
0.0061
-
N1-(4-(allyloxy) phenyl)-1-cyclopropanecarboxamide
-
pH 9.0, 20C
0.0129
-
N1-(4-(allyloxy) phenyl)-2-methylpropanamide
-
pH 9.0, 20C
0.0081
-
N1-(4-(allyloxy) phenyl)-3-chlorobenzamide
-
pH 9.0, 20C
0.0056
-
N1-(4-(allyloxy) phenyl)-3-fluorobenzamide
-
pH 9.0, 20C
0.017
-
N1-(4-(allyloxy) phenyl)-3-methoxybenzamide
-
pH 9.0, 20C
0.0067
-
N1-(4-(allyloxy) phenyl)-3-methylbenzamide
-
pH 9.0, 20C
0.0088
-
N1-(4-(allyloxy) phenyl)-4-chlorobenzamide
-
pH 9.0, 20C
0.0038
-
N1-(4-(allyloxy) phenyl)-4-fluorobenzamide
-
pH 9.0, 20C
0.0138
-
N1-(4-(allyloxy) phenyl)-4-methoxybenzamide
-
pH 9.0, 20C
0.0101
-
N1-(4-(allyloxy) phenyl)-4-methylbenzamide
-
pH 9.0, 20C
0.0033
-
N1-(4-(allyloxy) phenyl)benzamide
-
pH 9.0, 20C
0.04
-
nordihydroguaiaretic acid
-
at pH 9.0
0.0019
-
pentyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.59
-
peonidin
-
-
31
-
peonidin 3-O-arabinoside
-
-
37.7
-
peonidin 3-O-galactoside
-
-
37.5
-
peonidin 3-O-glucoside
-
-
0.0116
-
propyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.0048
-
quercetin
-
in 0.1M Tris-HCl (pH 8.0), at 25C
0.0357
-
sec-butyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
0.0387
-
tert-butyl 2-(4-methoxyphenyl)acetate
-
pH 9.0, 20C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10.2
-
-
crude extract, with linoleic acid as substrate
12
-
-
crude extract, with alpha-linolenic acid as substrate
23.4
-
B6D1W5
26fold purified enzyme, with linoleic acid as substrate
28.3
-
-
purified recombinant enzyme, pH 7.5, 25C
474
-
-
55fold purified enzyme, with alpha-linolenic acid as substrate
564
-
-
55fold purified enzyme, with linoleic acid as substrate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
8.5
B2IZG6
broad optimum with a maximum at pH 8.0, substrate: linoleate
4.8
-
Q27PX2
-
6
-
B6D1W5
-
6.25
-
-
isoform Oep1LOX2
6.3
-
-
isoenzyme Oep2LOX2
6.75
-
-
isoform Oep2LOX2
6.8
-
-
isoenzyme Oep1LOX2
7
9
-
linoleic acid is a considerably better substrate for SBLO-1 at pH 9.0 than at pH 7.0, while the activity with linoleyltrimethylammonium ion is the same at pH 7.0 and pH 9.0
7
-
P93184
-
7.2
-
-
triolein as substrate
7.5
-
-
recombinant enzyme
8
-
-
for alpha-linolenic acid
8.8
-
-
for linoleic acid
10
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8
-
activity range, overview
5.6
8.5
-
pH 5.6. about 50% of maximal activity, pH 8.5: about 70% of maximal activity
7
10.5
-
activity range, overview. Low activity below pH 7.0, maximum activity at pH 8.0, 75% of maximal activity at up to pH 10.5
7.8
8.4
-
at pH 7.8, ca. 50% of maximal activity, at pH 8.4, ca. 30% of maximal activity, substrate alpha-linoleic acid
8.5
8.9
-
at pH 8.5, ca. 30% of maximal activity, at pH 8.9, ca. 80% of maximal activity, substrate linolenic acid
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperaature
25
-
P93184
assay at
25
-
-
recombinant enzyme
25
-
-
assay at
35
-
-
isoenzyme Oep2LOX2; isoform Oep2LOX2
45
-
-
isoenzyme Oep1LOX2; isoform Oep1LOX2
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
55
-
more than 85% of maximal activity in the temperature-range: 15-55C, isoenzyme Oep1LOX2; recombinant Oep1LOX2 exhibits more than 85% of its maximal activity, whereas Oep2LOX2 displays about 50-100% of its maximal activity
20
60
-
activity range, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
-
sequence analysis, isoform Oep2LOX2
5.95
-
B6D1W5
calculated from sequence
7.2
-
-
sequence analysis, isoform Oep1LOX2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
Lox2 and Lox3 are present to a lesser extent, compared to leaf
Manually annotated by BRENDA team
Ipomoea nil Choisy
-
-
-
Manually annotated by BRENDA team
B6D1W5
is mainly expressed at late developmental stages, two Lox genes expressed in black olives. Increase of the LOX activity at the end of the green stage and the turning stage of the olives, and the maximum is reached at the black stage
Manually annotated by BRENDA team
-
Oep1LOX2 predominantely expressed
Manually annotated by BRENDA team
-
LOX2 level starts to rise steadily up to 24 h after jasmonic acid treatment, maximal lox3 levels are attained around 30 min after wounding or jasmonic acid treatment
Manually annotated by BRENDA team
-, Q6X5R5, Q6X5R6
;
Manually annotated by BRENDA team
-
Oep2LOX2 shows the highest expression levels in mature mesocarp tissue
Manually annotated by BRENDA team
Fusarium oxysporum 4287
-
-
-
Manually annotated by BRENDA team
-
Lox3 is detected in roots, Lox2 levels in roots is below limit of detection
Manually annotated by BRENDA team
-
restricted to uninfected cortical cells
Manually annotated by BRENDA team
-
Oep2LOX2 during development and ripening of Picual and Arbequina olive fruit
Manually annotated by BRENDA team
Q27PX2
low abundance in immature seeds
Manually annotated by BRENDA team
Q27PX2
low abundance in newly germinated seedlings
Manually annotated by BRENDA team
additional information
-
maximal enzyme production at growth temperature of 30C, activity increases gradually for plants between 15C and 30C but is slightly decreased when they are exposed to 30C or 35C
Manually annotated by BRENDA team
additional information
-
no obvious nodule-specific isoforms. Immunolocalisation of LOX protein
Manually annotated by BRENDA team
additional information
-
no obvious nodule-specific isoforms, the enzyme is detected in conglomerates at the cytosolic surface of amyloplasts. Immunolocalisation of LOX protein, overview
Manually annotated by BRENDA team
additional information
Ipomoea nil Choisy
-
maximal enzyme production at growth temperature of 30C, activity increases gradually for plants between 15C and 30C but is slightly decreased when they are exposed to 30C or 35C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is only found in the cytosol of uninfected cell types in the nodules
Manually annotated by BRENDA team
Pseudomonas aeruginosa BBE
-
-
-
-
Manually annotated by BRENDA team
additional information
-
lipid body
-
Manually annotated by BRENDA team
additional information
-
isoenzyme Oep1LOX2 and Oep2LOX2 contain an N-terminal chloroplastic transit peptide
-
Manually annotated by BRENDA team
additional information
-
no localization in plastids, immunolocalisation of LOX protein, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
95000
-
-
Western blotting and gel filtration
101700
-
-
sequence analysis, isoform Oep2LOX2
103400
-
-
sequence analysis, isoform Oep1LOX2
160000
-
-
about, recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
B6D1W5
x * 98000, SDS-PAGE and immunoblot; x * 98400, calculated from sequence
?
P93184
x * 106000, calculated from sequence
?
B2IZG6
x * 70891, calculated from sequence
?
-
x * 70000, SDS-PAGE
?
Nostoc punctiforme PCC73102
-
x * 70891, calculated from sequence
-
?
Pseudomonas aeruginosa BBE
-
x * 70000, SDS-PAGE
-
homodimer
-
2 * 8500, recombinant His-tagged enzyme, SDS-PAGE
homodimer
Fusarium oxysporum 4287
-
2 * 8500, recombinant His-tagged enzyme, SDS-PAGE
-
monomer
Q27PX2
1 * 105000, SDS-PAGE, His-tagged enzyme
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
65
-
purified extracellular enzyme, 25C, 7 min, stable at up to 35C, loss of 10% activity at 40C, and of 20% at 50C, 10% activity remaining at 60C, inactivation at 65C
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, 100 mM borate buffer, pH 10, 30% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, anion-exchange column chromatography and hydrophobic column chromatography
-
by sonication, centrifugation and gel filtration
-
by affinity chromatography; isoenzyme Oep1LOX2 and Oep2LOX2
-
by ammonium sulphate precipitation and ion-exchange chromatography, 55fold with a yield of 5.6%
-
by Ni-affinity chromatography and gel filtration, 26fold
B6D1W5
soluble LOX purified with His bind kits
Q27PX2
recombinant extracellular enzyme 13.5fold from Escherichia coli strain Rosetta (DE3) cell supernatant b two different steps of anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in insect cells; expression in insect cells; expression in insect cells; expression in insect cells; recombinant baculovirus expressing LOX2 (pFastBac) plasmid transferred into Escherichia coli DH10Bac containing the baculovirus shuttle vector bMON14272 and the helper plasmid pMON7124. Recombinant bacmid DNA transfected into High Five insect cells; recombinant baculovirus expressing LOX3 (pFastBac) plasmid transferred into Escherichia coli DH10Bac containing the baculovirus shuttle vector bMON14272 and the helper plasmid pMON7124. Recombinant bacmid DNA transfected into High Five insect cells; recombinant baculovirus expressing LOX4 (pFastBac) plasmid transferred into Escherichia coli DH10Bac containing the baculovirus shuttle vector bMON14272 and the helper plasmid pMON7124. Recombinant bacmid DNA transfected into High Five insect cells; recombinant baculovirus expressing LOX6 (pFastBac) plasmid transferred into Escherichia coli DH10Bac containing the baculovirus shuttle vector bMON14272 and the helper plasmid pMON7124. Recombinant bacmid DNA transfected into High Five insect cells
P38418, Q9CAG3, Q9FNX8, Q9LNR3
gene FoxLOX, DNA and amino acid sequence determination and analysis, phylogenetic analysis and sequence comparison, recombinnat expression of His-tagged enzyme
-
Escherichia coli BL21 cells carrying the plasmid PT7-7/L1 VTSLO-11
-
expressed in Escherichia coli BL21(DE3)pLysS and Rosetta(DE3)pLysS cells
-
into a pcDNA3.1 vector and introduced into HCT-116 and HT-29 cells
-
expression in Escherichia coli
P93184
expression in Escherichia coli
B2IZG6
isoenzyme Oep1LOX2 and Oep2LOX2; Oep1LOX2 and Oep2LOX2 ligated into vector pQE-80 L and overexpressed in Escherichia coli strain XL1-Blue
-
vector pQE30-LOX expressed in Escherichia coli M15 cells
B6D1W5
LOX1 ORF cloned into vector pET30a(+) for overexpression in Escherichia coli. LOX1-green GFP fusion construct, under the control of the cauliflower mosaic virus 35S promoter, expressed in Arabidopsis plants. Transgenic rice lines carrying either sense or antisense constructs under the control of a cauliflower mosaic virus 35S promoter
Q27PX2
overexpression and secretion of extracellular enzyme in Escherichia coli strain Rosetta(DE3) using the enzyme's endogenous signal peptide
-
gene tomloxD, overexpression in transgenic tomato plants, introduction of the binary vector pLoxD into Agrobacterium tumefaciens LBA4404 by the freeze-thaw method, phenotype, overview
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Lox is a low-expression gene, no expression in wild-type strain NRRL 3357
B5SXD0
Lox is expressed in the complemented strains TSHB3.1C and TSHB3.5C. While complemented strain TSHB3.1C (harboring a single-copy insertion) expresses a clear transcript, complemented strain TSHB3.5C (harboring at least two copies of lox and likely more) produces a greatly increased transcript and also produces an additional smaller band, which is absent in the single-copy strain TSHB3.1C
B5SXD0
0.04 mM honokiol markedly activates cellular 15-LOX-1 expression
-
cadmium induces lipoxygenase activity
-
the LOX2 gene is upregulated after wounding plus water and wounding plus Manduca sexta oral secretions treatment; the LOX3 gene is upregulated after wounding plus water and wounding plus Manduca sexta oral secretions treatment
-, Q6X5R5, Q6X5R6
Oep2LOX2 transcript levels increase in Picual and Arbequina mesocarps during development and ripening, showing a maximum at turning stage, whereas Oep1LOX2 exhibits constant expression levels in both olive varieties and tissues
-
in all antisense transgenic rice lines and more than half of the sense lines the expression levels of LOX1, the levels of enzyme activity, and the levels of the endogenous LOX1 products (jasmonic acid, (Z)-3-hexenal and colneleic acid) at 6, 48, and 48 h after brown planthopper feeding respectively, are below the levels found in non-transgenic control plants
Q27PX2
LOX1 transcripts accumulate rapidly and transiently in response to wounding or brown planthopper attack, reaching a peak 3 h after wounding and 6 h after insect feeding. Transgenic rice lines show altered LOX1 activity
Q27PX2
expression of the tomato gene encoding 13-lipoxygenase, TomloxD, is stimulated by wounding, pathogen infection, jasmonate, and systemin
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
B5SXD0
deletion of lox greatly diminishes density-dependent development of both sclerotia and conidia, resulting in an overall increase in the number of sclerotia and a decrease in the number of conidia at high cell densities. Lox mutants show decreased linoleic acid LOX activity
Q599H
B7FDE5, -
converts the enzyme to a pure 13-LOX
additional information
-
generation of transgenic tomato plants with greatly increased TomloxD content using sense constructs under the control of the CaMV 35S promoter. Expression levels of defense genes LeHSP90, LePR1, LePR6 and LeZAT in the transformants are higher than those in non-transformed plants, realtime RT-PCR expression analysis, overview. Transgenic plants harboring TomloxD are more tolerant to Cladosporium fulvum and high temperature stress than non-transformed tomato plants
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
the LOX/4-nitroso-N,N-dimethylaniline method is able to highlight high antioxidant activity values in durum wheat grains, as well as synergistic interactions among antioxidants from different extracts, and so provide a more comprehensive and integrated determination of antioxidant activity, which is essential for a total antioxidant activity assessment and may provide a more realistic quantification of food antioxidant effectiveness in preventing diseases
medicine
-
15-LO-1 expression in colorectal carcinoma may contribute to the inhibition of metastatic capacity in vitro and can be exploited for therapeutic purposes
food industry
-
lipoxygenase is widely used in food industry to improve aroma, rheological, or baking properties of foods
food industry
Pseudomonas aeruginosa BBE
-
lipoxygenase is widely used in food industry to improve aroma, rheological, or baking properties of foods
-
biotechnology
-
the tomloxD gene encoding the enzyme has potential applications in engineering cropping plants that are resistant to biotic and/or abiotic stress factors
medicine
-
induction of 15-LOX-1-mediated down-regulation of a PPAR-gamma and COX-2 pathway by honokiol is a therapeutic strategy for gastric cancer
additional information
Q27PX2
the manipulating of the expression of the LOX gene may provide a basis for advancing both the fundamental and applied biology of rice