Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(15S)-hydroperoxyeicosatetraenoic acid + O2
(8S,15S)-dihydroperoxyeicosatetraenoic acid + (5S,15S)-dihydroperoxyeicosatetraenoic acid
-
-
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetra-5,8,11,14-enoic acid + O2
?
(6Z,9Z,12Z)-octadeca-6,9,12-trienoic acid + O2
?
-
-
-
-
?
(7Z,10Z,13Z)-hexadecatrienoic acid + O2
?
-
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
?
(9Z,12Z,15Z)-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
alpha-linolenate + O2
(9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
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-linolenate + O2
13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
?
alpha-linolenic acid + O2
13-S-hydroperoxyoctadeca-9, 11,15-trienoic acid
alpha-linolenic acid + O2
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(12S)-12-hydroperoxyicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonic acid + O2
(5Z,8Z,11Z, 13E,15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
15-(S)-hydroperoxy-5(Z),8(Z),11(Z),13(E)-eicosatetraenoic acid
isoform LOX2 shows 50% activity compared to alpha-linolenic acid
-
-
?
docosahexaenoic acid + O2
?
gamma-linolenate + O2
(6Z,9Z,11E,13S)-13-hydroperoxy-6,9,11-octadecatrienoate
-
-
-
?
gamma-linolenate + O2
?
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
linoleate + O2
(9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
linoleate + O2
13-hydroperoxyoctadeca-9,11-dienoate
linoleate + O2
9-hydroperoxy octadecadienoic acid + 13-hydroperoxy octadecadienoic acid
linoleic acid + O2
(10E,12Z)-13-hydroperoxy-10,12-octadecadienoate
preferred substrate
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
linoleic acid + O2
13(S)-hydroperoxy-9,11-octadecadienoic acid
-
-
-
-
?
linoleic acid + O2
13(S)-hydroxyoctadecadienoic acid
-
-
-
-
?
linoleic acid + O2
13-hydroxy-12-oxo-9-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + 12-oxo-10-phytoenoic acid + 10-oxo-phytoenoic acid
-
-
combination of 9- and 13-lipoxygenases, ratio 10:2:1:3
-
?
linolenate + O2
?
the enzyme oxygenates linolenic acid more effectively than linoleic acid
the product is not determined
-
?
linolenic acid + O2
13(S)-hydroperoxylinolenic acid
-
-
-
-
?
linoleyltrimethylammonium ion + O2
13-hydroperoxy-(9Z,11E,13S)-octadecadienyltrimethylammonium ion
-
-
primarily
-
?
N-linolenoylethanolamide + O2
?
-
-
-
-
?
N-linoleoylethanolamide + O2
?
-
-
-
-
?
additional information
?
-
(5Z,8Z,11Z,14Z)-eicosatetra-5,8,11,14-enoic acid + O2
?
-
-
-
-
?
(5Z,8Z,11Z,14Z)-eicosatetra-5,8,11,14-enoic acid + O2
?
-
-
-
-
?
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
?
-
-
-
-
?
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
?
-
-
-
-
?
(9Z,12Z,15Z)-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
(9Z,12Z,15Z)-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
alpha-linolenate is the preferred substrate
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
Lox2 and Lox3 are more active against linolenate compared to linoleate
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenic acid + O2
13-S-hydroperoxyoctadeca-9, 11,15-trienoic acid
-
-
-
?
alpha-linolenic acid + O2
13-S-hydroperoxyoctadeca-9, 11,15-trienoic acid
100% activity
-
-
?
alpha-linolenic acid + O2
?
-
minor substrate
-
-
?
alpha-linolenic acid + O2
?
-
-
-
-
?
aniline blue + O2
?
69.7% decolorization after 35 min incubation
-
-
?
aniline blue + O2
?
69.7% decolorization after 35 min incubation
-
-
?
arachidonate + O2
?
-
-
-
-
?
arachidonate + O2
?
-
-
-
-
?
arachidonic acid + O2
?
isoform LOX3 shows 5% activity compared to alpha-linolenic acid
-
-
?
arachidonic acid + O2
?
isoform LOX4 shows 4% activity compared to alpha-linolenic acid
-
-
?
arachidonic acid + O2
?
isoform LOX6 shows 8% activity compared to alpha-linolenic acid
-
-
?
arachidonic acid + O2
?
-
-
-
?
arachidonic acid + O2
?
-
-
-
?
arachidonic acid + O2
?
very low activity and specific activity towards arachidonic acid
-
-
?
docosahexaenoic acid + O2
?
isoform LOX2 shows 56% activity compared to alpha-linolenic acid
-
-
?
docosahexaenoic acid + O2
?
isoform LOX3 shows 7% activity compared to alpha-linolenic acid
-
-
?
docosahexaenoic acid + O2
?
isoform LOX4 shows 8% activity compared to alpha-linolenic acid
-
-
?
docosahexaenoic acid + O2
?
isoform LOX6 shows 31% activity compared to alpha-linolenic acid
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
lipoxygenase 2 specifically oxidizes linoleate into 13-hydroperoxide
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
primary product
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
(9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
-
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)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
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
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
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
-
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
-
-
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
-
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
-
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
-
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-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
product identification by HPLC of recombinant extracellular enzyme, overview
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
product identification by HPLC of recombinant extracellular enzyme, overview
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
13-hydroperoxyoctadeca-9,11-dienoate
the isozyme is specific for formation of the 13-H(p)ODE isomer (94%),very low 9-H(p)ODE activity (6%)
-
-
?
linoleate + O2
9-hydroperoxy octadecadienoic acid + 13-hydroperoxy octadecadienoic acid
-
-
9-hydroperoxy octadecadienoic acid is the product of EC 1.13.11.58
-
?
linoleate + O2
9-hydroperoxy octadecadienoic acid + 13-hydroperoxy octadecadienoic acid
-
-
9-hydroperoxy octadecadienoic acid is the product of EC 1.13.11.58
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
-
4-nitroso-N,N-dimethylaniline bleaching in the course of linoleate hydroperoxidation by soybean LOX-1
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
-
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
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoic acid
-
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
-
preferred substrate
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
best substrate
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
best substrate
-
-
?
linoleic acid + O2
?
isoform LOX2 shows 79% activity compared to alpha-linolenic acid
-
-
?
linoleic acid + O2
?
isoform LOX3 shows 12% activity compared to alpha-linolenic acid
-
-
?
linoleic acid + O2
?
isoform LOX4 shows 11% activity compared to alpha-linolenic acid
-
-
?
linoleic acid + O2
?
isoform LOX6 shows 17% activity compared to alpha-linolenic acid
-
-
?
linoleic acid + O2
?
-
-
-
-
?
linolenic acid + O2
?
LOX-2 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
LOX-3 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
LOX-4 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
LOX-6 displays a selective oxygenation of linolenic acid
-
-
?
linolenic acid + O2
?
-
-
-
?
linolenic acid + O2
?
-
-
-
-
?
linolenic acid + O2
?
-
-
-
?
linolenic acid + O2
?
good preference for linolenic acid
-
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
additional information
?
-
arachidonic acid is a poor substrate
-
-
?
additional information
?
-
-
arachidonic acid is a poor substrate
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the optimal substrate concentration in the enzyme assay is 20 g/l
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the optimal substrate concentration in the enzyme assay is 20 g/l
-
-
?
additional information
?
-
-
oxygenation of triolein by lipid body LOX leads to a trihydroperoxy derivative
-
-
?
additional information
?
-
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
?
additional information
?
-
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
?
additional information
?
-
-
no activity with oleic 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
?
-
-
identification of products, by biotransformation and mass spectrometry, determination of the stereochemistry of the major product, overview
-
-
?
additional information
?
-
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
?
-
-
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
?
-
regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX
-
-
?
additional information
?
-
-
regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX
-
-
?
additional information
?
-
the enzyme also converts arachidonate to its (15S)-hydroperoxide. The enzyme shows no substrate preference
-
-
?
additional information
?
-
-
the enzyme also converts arachidonate to its (15S)-hydroperoxide. The enzyme shows no substrate preference
-
-
?
additional information
?
-
the enzyme also converts linolenate into the 13-hydroperoxyy fatty acid
-
-
?
additional information
?
-
-
the enzyme also converts linolenate into the 13-hydroperoxyy fatty acid
-
-
?
additional information
?
-
-
mitochondrial membrane oxygenase activity of the enzyme PA-LOX, overview. PA-LOX is capable of oxygenating both, arachidonic acid and linoleic acid, the two major polyenoic fatty acids found in animal biomembranes. The enzyme binds phospholipids at its active site
-
-
?
additional information
?
-
-
LOXs catalyze the regio- and stereospecific dioxygenation of polyunsaturated fatty acids with a (1Z,4Z)-pentadiene structure
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
alpha-linolenate + O2
13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
?
alpha-linolenic acid + O2
13-S-hydroperoxyoctadeca-9, 11,15-trienoic acid
-
-
-
?
arachidonic acid + O2
(5Z,8Z,11Z, 13E,15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid
-
-
-
-
?
gamma-linolenate + O2
?
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
linoleate + O2
(9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
linoleate + O2
13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
9-hydroperoxy octadecadienoic acid + 13-hydroperoxy octadecadienoic acid
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
linolenic acid + O2
13(S)-hydroperoxylinolenic acid
-
-
-
-
?
linolenic acid + O2
?
-
-
-
?
additional information
?
-
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
all-cis-9,12,15-octadecatrienoic acid + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
alpha-linolenate + O2
(9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
-
-
-
-
?
arachidonate + O2
?
-
-
-
-
?
arachidonate + O2
?
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
lipoxygenase 2 specifically oxidizes linoleate into 13-hydroperoxide
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
9-hydroperoxy octadecadienoic acid + 13-hydroperoxy octadecadienoic acid
-
-
9-hydroperoxy octadecadienoic acid is the product of EC 1.13.11.58
-
?
linoleate + O2
9-hydroperoxy octadecadienoic acid + 13-hydroperoxy octadecadienoic acid
-
-
9-hydroperoxy octadecadienoic acid is the product of EC 1.13.11.58
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
-
?
additional information
?
-
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
?
additional information
?
-
-
product specificity of FoxLOX, by SP-HPLC/DAD analysis, overview
-
-
?
additional information
?
-
-
mitochondrial membrane oxygenase activity of the enzyme PA-LOX, overview. PA-LOX is capable of oxygenating both, arachidonic acid and linoleic acid, the two major polyenoic fatty acids found in animal biomembranes. The enzyme binds phospholipids at its active site
-
-
?
additional information
?
-
-
LOXs catalyze the regio- and stereospecific dioxygenation of polyunsaturated fatty acids with a (1Z,4Z)-pentadiene structure
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-(cyclohexylmethyl)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-(cyclohexylemethyl)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'-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
-
-
4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
-
-
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
adamantyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.074 mM
-
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
bornyl vanillate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.401 mM
-
butyl 2-(4-methoxyphenyl)acetate
-
-
catechin
-
competitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
Cd2+
complete inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM
cis-(+)-12-oxophytodienoic acid
isoform LOX2 exhibits 64% residual activity at 2.8 mM; isoform LOX3 exhibits 60% residual activity at 2.8 mM; isoform LOX4 exhibits 21% residual activity at 2.8 mM; isoform LOX6 exhibits 50% residual activity at 2.8 mM
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
ethyl 2-(4-methoxyphenyl)acetate
-
-
fenchyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.089 mM
-
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
hexyl 2-(4-methoxyphenyl)acetate
-
-
isobutyl 2-(4-methoxyphenyl)acetate
-
-
isopropyl 2-(4-methoxyphenyl)acetate
-
-
K+
38% residual activity at 50 mM
L-ascorbic acid
-
noncompetitive inhibition of the LOX/4-nitroso-N,N-dimethylaniline reaction
methyl jasmonate
isoform LOX2 exhibits 87% residual activity at 2.8 mM; isoform LOX3 exhibits 85% residual activity at 2.8 mM; isoform LOX4 exhibits 95% residual activity at 2.8 mM; isoform LOX6 exhibits 94% residual activity at 2.8 mM
N-(cyclohexylmethyl)-2-{3-[hydroxy(phenyl)methyl]phenyl}propanamide
-
-
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-cyclohexyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
N-cyclopentyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
-
-
N-ethylmaleimide
isoform LOX2 exhibits 84% residual activity at 2.8 mM; isoform LOX3 exhibits 51% residual activity at 2.8 mM; isoform LOX4 exhibits 11% residual activity at 2.8 mM; isoform LOX6 exhibits 47% residual activity at 2.8 mM
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
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
-
-
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
Salicylhydroxamic acid
70% inhibition in the presence of 1 mM salicylhydroxamic acid
salicylic acid
isoform LOX2 exhibits 96% residual activity at 2.8 mM
sec-butyl 2-(4-methoxyphenyl)acetate
-
-
stylosin
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.101 mM
-
tert-butyl 2-(4-methoxyphenyl)acetate
-
-
traumatic acid
isoform LOX2 exhibits 95% residual activity at 2.8 mM
-
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
Cu2+
complete inhibition at 1 mM; complete inhibition at 1 mM; complete inhibition at 1 mM; isoform LOX2 exhibits 50% residual activity at 1 mM
Cu2+
-
required for optimal activity, activates at 0.1 mM, inhibits at 1 mM
Cu2+
-
about 70% inhibition at 20 mM
Cu2+
-
inhibits Oep2LOX2 by 49%
Fe3+
complete inhibition at 10 mM
Fe3+
-
slight inactivation
Hg2+
-
about 80% inhibition at 20 mM
Hg2+
-
inhibits Oep1LOX2 by 60% and totally inactivates Oep2LOX2
nordihydroguaiaretic acid
-
-
nordihydroguaiaretic acid
is a noncompetitive inhibitor
propyl gallate
is a competitive inhibitor
propyl gallate
almost complete inhibition (99%) in the presence of 1 mM propyl gallate
Zn2+
-
activates at 1 mM, inhibits at 0.1 mM
Zn2+
-
complete inhibition at 20 mM
Zn2+
53% residual activity at 50 mM
additional information
isoform LOX3 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid
-
additional information
isoform LOX3 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid
-
additional information
isoform LOX3 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid
-
additional information
isoform LOX3 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid; isoform LOX4 is not inhibited by traumatic acid and salicylic acid
-
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
-
additional information
stylosin and some similar synthetic monoterpenoids show inhibitory effects on 15-LOX. A strong positive correlation is observed between 15-LOX inhibition potential and cytotoxicity of the compounds with apoptosis being the predominant mechanism of induced cell death
-
additional information
-
stylosin and some similar synthetic monoterpenoids show inhibitory effects on 15-LOX. A strong positive correlation is observed between 15-LOX inhibition potential and cytotoxicity of the compounds with apoptosis being the predominant mechanism of induced cell death
-
additional information
-
enzyme LOX1 is not inhibited by jasmonic acid; enzyme LOX2 is not inhibited by jasmonic acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.033
1-(4-methoxyphenyl)-2-butanone
Glycine max
-
pH 9.0, 20°C
0.043
1-(4-methoxyphenyl)acetone
Glycine max
-
pH 9.0, 20°C
0.145
1-methoxy-4-(2-ethylallyl)benzene
Glycine max
-
pH 9.0, 20°C
0.137
1-methoxy-4-(2-methylallyl)benzene
Glycine max
-
pH 9.0, 20°C
0.1
2',4,6-trimethoxy-aurone
Glycine max
-
at pH 9.0
0.1
2'-hydroxy-2-methoxy-chalcone
Glycine max
-
at pH 9.0
0.0675
2'-hydroxy-3,4-dimethoxy-chalcone
Glycine max
-
at pH 9.0
0.082
2'-hydroxy-4-chloro-4', 6'-dimethoxy-chalcone
Glycine max
-
at pH 9.0
0.056
2'-hydroxy-4-chloro-chalcone
Glycine max
-
at pH 9.0
0.053
2'-hydroxy-4-methyl-4',6'-dimethoxy-chalcone
Glycine max
-
at pH 9.0
0.0525
2'-hydroxy-4-methyl-chalcone
Glycine max
-
at pH 9.0
0.12
2-(3-(hydroxy(phenyl)methyl)phenyl)-N-phenethylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.13
2-(3-(hydroxy(phenyl)methyl)phenyl)propanoic acid
Glycine max
-
25°C, pH not specified in the publication
0.053
2-(3-benzoylphenyl)-N-(cyclohexylmethyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.12
2-(3-benzoylphenyl)-N-cyclohexylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.0615
2-(3-benzoylphenyl)-N-cyclopentylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.065
2-(3-benzoylphenyl)-N-phenethylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.4
2-(3-benzylphenyl)-N,N-bis(2-hydroxyethyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.27
2-(3-benzylphenyl)-N-(2-hydroxyethyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.28
2-(3-benzylphenyl)-N-(3-hydroxypropyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.08
2-(3-benzylphenyl)-N-(cyclohexylemethyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.0375
2-(3-benzylphenyl)-N-cyclohexylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.082
2-(3-benzylphenyl)-N-cyclopentylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.385
2-(3-benzylphenyl)-N-ethoxypropanamide
Glycine max
-
25°C, pH not specified in the publication
0.043
2-(3-benzylphenyl)-N-phenethylpropanamide
Glycine max
-
25°C, pH not specified in the publication
0.325
2-(3-benzylphenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.415
2-(3-benzylphenyl)propanoic acid
Glycine max
-
25°C, pH not specified in the publication
0.00207
2-dodecyl-6-hydroxybenzoic acid
Glycine max
-
pH 9.0
0.0068
2-hydroxy-6-[(8E)-pentadec-8-en-1-yl]benzoic acid
Glycine max
-
pH 9.0
0.07
4'-methoxy-aurone
Glycine max
-
at pH 9.0
0.05
4,4',6-trimethoxy-aurone
Glycine max
-
at pH 9.0
0.0062
4-(allyloxy)phenyl benzoate
Glycine max
-
pH 9.0, 20°C
0.0067
4-allylphenyl benzoate
Glycine max
-
pH 9.0, 20°C
0.0562
4-Methoxyphenylacetic acid
Glycine max
-
pH 9.0, 20°C
0.0171
4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
Homo sapiens
pH 7.0, 25°C
-
0.0188
6-(2'-ethylheptyl)salicylic acid
Glycine max
-
pH 9.0
0.0105
6-(4',8'-dimethylnonyl) salicylic acid
Glycine max
-
pH 9.0
0.0143
6-pentadecanylsalicylic acid
Glycine max
-
pH 9.0
0.4
6-[2'-(2'',5''-dihydroxyphenyl)ethyl]salicylic acid
Glycine max
-
pH 9.0
0.0261
adamantyl caffeate
Homo sapiens
pH 7.0, 25°C
-
0.0078
beta-carotene
Glycine max
-
-
0.399
bornyl vanillate
Homo sapiens
pH 7.0, 25°C
-
0.0038
butyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.048 - 2.8
cis-(+)-12-oxophytodienoic acid
1
Cu2+
Arabidopsis thaliana
isoform LOX2, at pH 7.2 and 25°C
0.58
cyanidin
Glycine max
-
-
1.24
cyanidin 3-O-arabinoside
Glycine max
-
-
0.18
cyanidin 3-O-galactoside
Glycine max
-
-
0.25
cyanidin 3-O-glucoside
Glycine max
-
-
0.064
cyclohexyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.0565
cyclopentyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.27
delphinidin
Glycine max
-
-
0.49
delphinidin 3-O-arabinoside
Glycine max
-
-
0.00046
delphinidin 3-O-galactoside
Glycine max
-
-
0.00043
delphinidin 3-O-glucoside
Glycine max
-
-
0.0641
esteragol
Glycine max
-
pH 9.0, 20°C
0.0641
estragol
Glycine max
-
pH 9.0, 20°C
0.032
ethyl 2-(4-methoxyphenyl)acetate
Glycine max
-
-
0.0382
eugenol
Glycine max
-
pH 9.0, 20°C
0.007
eugenyl benzoate
Glycine max
-
pH 9.0, 20°C
0.011
fenchyl caffeate
Homo sapiens
pH 7.0, 25°C
-
0.0197
glutathione
Glycine max
-
-
0.035
hexyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.0881
isobutyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.0344
isopropyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.13
Ketoprofen
Glycine max
-
25°C, pH not specified in the publication
0.0961
methyleugenol
Glycine max
-
pH 9.0, 20°C
0.295
N-(cyclohexylmethyl)-2-{3-[hydroxy(phenyl)methyl]phenyl}propanamide
Glycine max
-
25°C, pH not specified in the publication
0.0205
N-benzhydryl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.0645
N-benzhydryl-2-(3-benzoylphenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.05
N-benzhydryl-2-(3-benzylphenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.2
N-benzyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.0875
N-benzyl-2-(3-benzoylphenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.0745
N-benzyl-2-(3-benzylphenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.1
N-benzyloxy-2-(3-benzylphenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.425
N-cyclohexyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.23
N-cyclopentyl-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.2
N-hydroxy-2-(3-(hydroxy(phenyl)methyl)phenyl)propanamide
Glycine max
-
25°C, pH not specified in the publication
0.00067
N1-(4-(allyloxy) phenyl)-1-admantancarboxamide
Glycine max
-
pH 9.0, 20°C
0.0022
N1-(4-(allyloxy) phenyl)-1-cyclobutanecarboxamide
Glycine max
-
pH 9.0, 20°C
0.0064
N1-(4-(allyloxy) phenyl)-1-cyclohexanecarboxamide
Glycine max
-
pH 9.0, 20°C
0.0041
N1-(4-(allyloxy) phenyl)-1-cyclopantanecarboxamide
Glycine max
-
pH 9.0, 20°C
0.0061
N1-(4-(allyloxy) phenyl)-1-cyclopropanecarboxamide
Glycine max
-
pH 9.0, 20°C
0.0129
N1-(4-(allyloxy) phenyl)-2-methylpropanamide
Glycine max
-
pH 9.0, 20°C
0.0081
N1-(4-(allyloxy) phenyl)-3-chlorobenzamide
Glycine max
-
pH 9.0, 20°C
0.0056
N1-(4-(allyloxy) phenyl)-3-fluorobenzamide
Glycine max
-
pH 9.0, 20°C
0.017
N1-(4-(allyloxy) phenyl)-3-methoxybenzamide
Glycine max
-
pH 9.0, 20°C
0.0067
N1-(4-(allyloxy) phenyl)-3-methylbenzamide
Glycine max
-
pH 9.0, 20°C
0.0088
N1-(4-(allyloxy) phenyl)-4-chlorobenzamide
Glycine max
-
pH 9.0, 20°C
0.0038
N1-(4-(allyloxy) phenyl)-4-fluorobenzamide
Glycine max
-
pH 9.0, 20°C
0.0138
N1-(4-(allyloxy) phenyl)-4-methoxybenzamide
Glycine max
-
pH 9.0, 20°C
0.0101
N1-(4-(allyloxy) phenyl)-4-methylbenzamide
Glycine max
-
pH 9.0, 20°C
0.0033
N1-(4-(allyloxy) phenyl)benzamide
Glycine max
-
pH 9.0, 20°C
0.04
nordihydroguaiaretic acid
Glycine max
-
at pH 9.0
0.0019
pentyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.59
peonidin
Glycine max
-
-
31
peonidin 3-O-arabinoside
Glycine max
-
-
37.7
peonidin 3-O-galactoside
Glycine max
-
-
37.5
peonidin 3-O-glucoside
Glycine max
-
-
0.0116
propyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.0048
quercetin
Glycine max
-
in 0.1M Tris-HCl (pH 8.0), at 25°C
0.0357
sec-butyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.0668
stylosin
Homo sapiens
pH 7.0, 25°C
-
0.0387
tert-butyl 2-(4-methoxyphenyl)acetate
Glycine max
-
pH 9.0, 20°C
0.6
caffeic acid
Glycine max
-
at pH 9.0
0.6
caffeic acid
Glycine max
-
25°C, pH not specified in the publication
0.048
cis-(+)-12-oxophytodienoic acid
Arabidopsis thaliana
isoform LOX4, at pH 7.2 and 25°C
2.8
cis-(+)-12-oxophytodienoic acid
Arabidopsis thaliana
isoform LOX6, at pH 7.2 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
DNA and amino acid sequence determination and analysis of LOX1 and LOX2 isozymes, phylogenetic analysis, only LOX1:Md:1a exhibits a glycine residue (Gly567) responsible for dual positional specificity and (R)-LOX activity
evolution
genes CmLOX10 and CmLOX13 include all of the typical LOX domains and share 58.11% identity at the amino acid level with each other. The phylogenetic analysis reveals that CmLOX10 and CmLOX13 are members of the type 2 13-LOX subgroup which are known to be involved in biotic and abiotic stress. The two lipoxygenases may play different functions in oriental melon during plant growth and development, CmLOX10 and CmLOX13 enzyme reaction shows that both enzymes produce 13S-hydroperoxides when linoleic acid is used as substrate
malfunction
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
reduced LOX2 expression decreases the release of green leaf volatiles but does not impair jasmonic acid and jasmonic acid-Ile accumulation
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
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
metabolism
-
13-hydroxy-9,11,5-octadecatrienoic acid (13-HOTrE) is produced by the reduction of a 13-LOX product, 13-hydroperoxy-9,11,15-octadecatrienoic acid (by peroxidases), one of the key substrates of jasmonate biosynthesis
metabolism
-
profiling of oxylipins from young maize roots reveals complex patterns of products mainly originating from the combined actions of 9- and 13-lipoxygenases and allene oxide synthase. A distinctive feature is the high content of the cyclopentenone 10-oxo-11-phytoenoic acid (10-oxo-PEA)
metabolism
the enzyme is involved in the LOX pathway, overview
physiological function
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
-
involvement of Cd-induced LOX activity in the premature differentiation of the barley root tip during Cd stress
physiological function
LOX-2 is a 13S-lipoxygenases, it has no dual positional specificity
physiological function
LOX-3 is a 13S-lipoxygenases, it has no dual positional specificity
physiological function
LOX-4 is a 13S-lipoxygenases, it has no dual positional specificity
physiological function
LOX-6 is a 13S-lipoxygenases, it has no dual positional specificity
physiological function
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
-
major involvement of the Oep2LOX2 gene in the biosynthesis of virgin olive oil aroma compounds
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
-
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
physiological function
lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus domestica) fruit upon tissue disruption, role in autonomously produced aroma volatiles from intact tissue, overview. The genetic association with a quantitative trait locus for fruit ester and the remarkable agreement in regio- and stereoselectivity of the LOX1:Md:1a reaction with the overall LOX activity found in mature apple fruits, suggest a major physiological function of LOX1:Md:1a during climacteric ripening of apples. While isozymes LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b may contribute to aldehyde production in immature fruit upon cell disruption isozyme, LOX1:Md:1a probably regulates the availability of precursors for ester production in intact fruit tissue. Both 9- and 13-hydroperoxides can be catabolized to aroma-active volatile aldehydes by hydroperoxide lyase. Only 13-LOX activity contributes to the apple aroma due to the formation of precursors of C6 volatile compounds. The dioxygenation of PUFAs by 9- and 13-LOX activity forms precursors for important phytooxylipins with functions in plant defense, wound signaling, senescence and fruit ripening
physiological function
-
secreted lipoxygenase from Pseudomonas aeruginosa exhibits biomembrane oxygenase activity and induces hemolysis in human red blood cells. Secreted lipoxygenase oxygenates free arachidonic acid predominantly to 15S-hydro(peroxy)-5Z,8Z,11Z,13E-eicosatetraenoic acid. The enzyme is capable of binding phospholipids at its active site and physically interacts with model membranes
physiological function
the isozyme CmLOX10 is involved in biotic and abiotic stress
physiological function
the isozyme CmLOX13 is involved in biotic and abiotic stress
physiological function
-
the lipoxygenase oxidizes linoleic acid into hydroperoxy octadecadienoic acid (HPOD), which is important in food and flavour industries for production of bread and flavouring compounds
physiological function
15 lipoxygenase 1 is abundant in asthmatic human airway epithelial cells and binds phosphatidylethanolamine-binding protein 1 (PEBP1), leading to generation of hydroperoxy-phospholipids, which drive ferroptotic cell death. 15LO1, PEBP1, and glutathione peroxidase 4 GPX4 activity drives abnormal asthmatic redox biology, to enhance type 2 inflammatory responses. In vitro, type 2 inflammatory cytokine IL-13 induces 15LO1 generation of hydroperoxy-phospholipids, which lowers intracellular GSH and increased extracellular GSSG levels. Lowering GSH further by inhibiting cystine transporter SLC7A11 enhances type 2 inflammatory protein expression and ferroptosis. Ex vivo, redox imbalances correspond to 15LO1 and SLC7A11 expression, type 2 inflammatory biomarkers, and worsen clinical outcomes
physiological function
eosinophils are the major cell type expressing 12/15-LOX during the corneal wound healing process. Eosinophils are recruited into the conjunctiva after corneal epithelium wounding, and eosinophil-deficient and/or eosinophil-specific 12/15-LOX knockout mice show delayed corneal wound healing compared with wild-type mice. A series of 12/15-LOX-derived mediators are significantly decreased in eosinophil-deficient mice and topical application of 17-hydroxydocosahexaenoic acid restores the phenotype
physiological function
-
the 13-lipoxygenase MSD2 does not function in herbivore-induced jasmonic acid production. The enzyme is important for producing jasmonic acid to regulate panicle development and spikelet fertility
physiological function
-
the enzyme plays a role in berry lipid peroxidation and possibly oxylipins synthesis
physiological function
-
the lipoxygenase oxidizes linoleic acid into hydroperoxy octadecadienoic acid (HPOD), which is important in food and flavour industries for production of bread and flavouring compounds
-
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
-
enzyme homology modeling using the crystal structure of linoleate 13-lipoxygenase from Pseudomonas aeruginosa, PDB entry 4G32, as a template
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
-
enzyme homology modeling using the crystal structure of linoleate 13-lipoxygenase from Pseudomonas aeruginosa, PDB entry 4G32, as a template
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
Horowitz Brown, S.; Zarnowski, R.; Sharpee, W.C.; Keller, N.P.
Morphological transitions governed by density dependence and lipoxygenase activity in Aspergillus flavus
Appl. Environ. Microbiol.
74
5674-5685
2008
Aspergillus flavus (B5SXD0), Aspergillus flavus
brenda
Palmieri-Thiers, C.; Canaan, S.; Brunini, V.; Lorenzi, V.; Tomi, F.; Desseyn, J.L.; Garscha, U.; Oliw, E.H.; Berti, L.; Maury, J.
A lipoxygenase with dual positional specificity is expressed in olives (Olea europaea L.) during ripening
Biochim. Biophys. Acta
1791
339-346
2009
Olea europaea (B6D1W5)
brenda
Jacquot, C.; Peng, S.; van der Donk, W.A.
Kinetic isotope effects in the oxidation of arachidonic acid by soybean lipoxygenase-1
Bioorg. Med. Chem. Lett.
18
5959-5962
2008
Glycine max
brenda
Seyedi, S.M.; Jafari, Z.; Attaran, N.; Sadeghian, H.; Saberi, M.R.; Riazi, M.M.
Design, synthesis and SAR studies of 4-allyoxyaniline amides as potent 15-lipoxygenase inhibitors
Bioorg. Med. Chem.
17
1614-1622
2009
Glycine max
brenda
Sadeghian, H.; Attaran, N.; Jafari, Z.; Saberi, M.R.; Pordel, M.; Riazi, M.M.
Design and synthesis of 4-methoxyphenylacetic acid esters as 15-lipoxygenase inhibitors and SAR comparative studies of them
Bioorg. Med. Chem.
17
2327-2335
2009
Glycine max
brenda
Detsi, A.; Majdalani, M.; Kontogiorgis, C.A.; Hadjipavlou-Litina, D.; Kefalas, P.
Natural and synthetic 2-hydroxy-chalcones and aurones: Synthesis, characterization and evaluation of the antioxidant and soybean lipoxygenase inhibitory activity
Bioorg. Med. Chem.
17
8073-8085
2009
Glycine max
brenda
Cimen, I.; Tuncay, S.; Banerjee, S.
15-Lipoxygenase-1 expression suppresses the invasive properties of colorectal carcinoma cell lines HCT-116 and HT-29
Cancer Sci.
100
2283-2291
2009
Homo sapiens
brenda
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
brenda
Feussner, I.; Bachmann, A.; Hhne, M.; Kindl, H.
All three acyl moieties of trilinolein are efficiently oxygenated by recombinant His-tagged lipid body lipoxygenase in vitro
FEBS Lett.
431
433-436
1998
Cucumis sativus
brenda
Pastore, D.; Laus, M.N.; Tozzi, D.; Fogliano, V.; Soccio, M.; Flagella, Z.
New tool to evaluate a comprehensive antioxidant activity in food extracts: Bleaching of 4-nitroso-N,N-dimethylaniline catalyzed by soybean lipoxygenase-1
J. Agric. Food Chem.
28
9682-9292
2009
Glycine max
brenda
Padilla, M.N.; Hernandez, M.L.; Sanz, C.; Martnez-Rivas, J.M.
Functional characterization of two 13-lipoxygenase genes from olive fruit in relation to the biosynthesis of volatile compounds of virgin olive oil
J. Agric. Food Chem.
57
9097-9107
2009
Olea europaea
brenda
Peng, Y.-L.; Shirono, Y.; Ohta, H.; Hibino, T.; Tanaka, K.; Shibata, D.
A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus
J. Biol. Chem.
269
3755-3761
1994
Oryza sativa (P38419), Oryza sativa
brenda
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
brenda
Bannenberg, G.; Martnez, M.; Hamberg, M.; Castresana, C.
Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana
Lipids
44
85-95
2008
Arabidopsis thaliana (P38418), Arabidopsis thaliana (Q9CAG3), Arabidopsis thaliana (Q9FNX8), Arabidopsis thaliana (Q9LNR3), Arabidopsis thaliana
brenda
Knaup, B.; Oehme, A.; Valotis, A.; Schreier, P.
Anthocyanins as lipoxygenase inhibitors
Mol. Nutr. Food Res.
53
617-624
2009
Glycine max
brenda
Bruinsma, M.; van Broekhoven, S.; Poelman, E.H.; Posthumus, M.A.; Mueller, M.J.; van Loon, J.J.; Dicke, M.
Inhibition of lipoxygenase affects induction of both direct and indirect plant defences against herbivorous insects
Oecologia
162
393-404
2010
Brassica oleracea var. gemmifera
brenda
Jacquot, C.; McGinley, C.M.; Plata, E.; Holman, T.R.; van der Donk, W.A.
Synthesis of 11-thialinoleic acid and 14-thialinoleic acid, inhibitors of soybean and human lipoxygenases
Org. Biomol. Chem.
6
4242-4252
2008
Glycine max
brenda
Lang, I.; Feussner, I.
Oxylipin formation in Nostoc punctiforme (PCC73102)
Phytochemistry
68
1120-1127
2007
Nostoc punctiforme (B2IZG6), Nostoc punctiforme
brenda
Williams, M.; Harwood, J.L.
Characterisation of lipoxygenase isoforms from olive callus cultures
Phytochemistry
69
2532-2538
2008
Olea europaea
brenda
Hornung, E.; Kunze, S.; Liavonchanka, A.; Zimmermann, G.; Khn, D.; Fritsche, K.; Renz, A.; Khn, H.; Feussner, I.
Identification of an amino acid determinant of pH regiospecificity in a seed lipoxygenase from Momordica charantia
Phytochemistry
69
2774-2780
2008
Momordica charantia (B7FDE5), Momordica charantia
brenda
Wang, R.; Shen, W.; Liu, L.; Jiang, L.; Liu, Y.; Su, N.; Wan, J.
A novel lipoxygenase gene from developing rice seeds confers dual position specificity and responds to wounding and insect attack
Plant Mol. Biol.
66
401-414
2008
Oryza sativa (Q27PX2), Oryza sativa
brenda
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
brenda
Kubo, I.; Ha, T.J.; Tsujimoto, K.; Tocoli, F.E.; Green, I.R.
Evaluation of lipoxygenase inhibitory activity of anacardic acids
Z. Naturforsch. C
63
539-546
2008
Glycine max
brenda
Osipova, E.V.; Lantsova, N.V.; Chechetkin, I.R.; Mukhitova, F.K.; Hamberg, M.; Grechkin, A.N.
Hexadecanoid pathway in plants: Lipoxygenase dioxygenation of (7Z,10Z,13Z)-hexadecatrienoic acid
Biochemistry (Moscow)
75
708-716
2010
Glycine max
brenda
Liu, S.H.; Shen, C.C.; Yi, Y.C.; Tsai, J.J.; Wang, C.C.; Chueh, J.T.; Lin, K.L.; Lee, T.C.; Pan, H.C.; Sheu, M.L.
Honokiol inhibits gastric tumourigenesis by activation of 15-lipoxygenase-1 and consequent inhibition of peroxisome proliferator-activated receptor-gamma and COX-2-dependent signals
Br. J. Pharmacol.
160
1963-1972
2010
Homo sapiens
brenda
Ha, T.J.; Shimizu, K.; Ogura, T.; Kubo, I.
Inhibition mode of soybean lipoxygenase-1 by quercetin
Chem. Biodivers.
7
1893-1903
2010
Glycine max
brenda
Rajic, Z.; Hadjipavlou-Litina, D.; Pontiki, E.; Kralj, M.; Suman, L.; Zorc, B.
The novel ketoprofen amides--synthesis and biological evaluation as antioxidants, lipoxygenase inhibitors and cytostatic agents
Chem. Biol. Drug Des.
75
641-652
2010
Glycine max
brenda
Keereetaweep, J.; Kilaru, A.; Feussner, I.; Venables, B.J.; Chapman, K.D.
Lauroylethanolamide is a potent competitive inhibitor of lipoxygenase activity
FEBS Lett.
584
3215-3222
2010
Glycine max
brenda
Zheng, Y.; Brash, A.R.
Formation of a cyclopropyl epoxide via a leukotriene A synthase-related pathway in an anaerobic reaction of soybean lipoxygenase-1 with 15S-hydroperoxyeicosatetraenoic acid: evidence that oxygen access is a determinant of secondary reactions with fatty acid hydroperoxides
J. Biol. Chem.
285
13427-13436
2010
Glycine max
brenda
Zheng, Y.; Brash, A.R.
On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1
J. Biol. Chem.
285
39876-39887
2010
Glycine max
brenda
Allmann, S.; Halitschke, R.; Schuurink, R.C.; Baldwin, I.T.
Oxylipin channelling in Nicotiana attenuata: lipoxygenase 2 supplies substrates for green leaf volatile production
Plant Cell Environ.
33
2028-2040
2010
Nicotiana attenuata (Q6X5R5), Nicotiana attenuata (Q6X5R6)
brenda
Lu, X.; Zhang, J.; Liu, S.; Zhang, D.; Xu, Z.; Wu, J.; Li, J.; Du, G.; Chen, J.
Overproduction, purification, and characterization of extracellular lipoxygenase of Pseudomonas aeruginosa in Escherichia coli
Appl. Microbiol. Biotechnol.
97
5793-5800
2013
Pseudomonas aeruginosa, Pseudomonas aeruginosa BBE
brenda
Chohany, L.E.; Bishop, K.A.; Camic, H.; Sup, S.J.; Findeis, P.M.; Clapp, C.H.
Cationic substrates of soybean lipoxygenase-1
Bioorg. Chem.
39
94-100
2011
Glycine max
brenda
Nam, K.H.; Yoshihara, T.
Interactions among LOX metabolites regulate temperature-mediated flower bud formation in morning glory (Pharbitis nil)
J. Plant Physiol.
169
1815-1820
2012
Ipomoea nil, Ipomoea nil Choisy
brenda
Demchenko, K.; Zdyb, A.; Feussner, I.; Pawlowski, K.
Analysis of the subcellular localisation of lipoxygenase in legume and actinorhizal nodules
Plant Biol.
14
56-63
2012
Casuarina glauca, Datisca glomerata
brenda
Hu, T.; Zeng, H.; Hu, Z.; Qv, X.; Chen, G.
Overexpression of the tomato 13-lipoxygenase gene TomloxD increases generation of endogenous jasmonic acid and resistance to Cladosporium fulvum and high temperature
Plant Mol. Biol. Rep.
31
1141-1149
2013
Solanum lycopersicum
-
brenda
Brodhun, F.; Cristobal-Sarramian, A.; Zabel, S.; Newie, J.; Hamberg, M.; Feussner, I.
An iron 13S-lipoxygenase with an alpha-linolenic acid specific hydroperoxidase activity from Fusarium oxysporum
PLoS ONE
8
e64919
2013
Fusarium oxysporum, Fusarium oxysporum 4287
brenda
Patel, D.D.; Patel, R.R.; Thakkar, V.R.
Purification, characterization and application of lipoxygenase isoenzymes from Lasiodiplodia theobromae
Appl. Biochem. Biotechnol.
175
513-525
2015
Lasiodiplodia theobromae, Lasiodiplodia theobromae MTCC 3068
brenda
An, J.U.; Kim, B.J.; Hong, S.H.; Oh, D.K.
Characterization of an omega-6 linoleate lipoxygenase from Burkholderia thailandensis and its application in the production of 13-hydroxyoctadecadienoic acid
Appl. Microbiol. Biotechnol.
99
5487-5497
2015
Burkholderia thailandensis, Burkholderia thailandensis KCTC 23190
brenda
Banthiya, S.; Pekarova, M.; Kuhn, H.; Heydeck, D.
Secreted lipoxygenase from Pseudomonas aeruginosa exhibits biomembrane oxygenase activity and induces hemolysis in human red blood cells
Arch. Biochem. Biophys.
584
116-124
2015
Pseudomonas aeruginosa
brenda
Ogorodnikova, A.V.; Gorina, S.S.; Mukhtarova, L.S.; Mukhitova, F.K.; Toporkova, Y.Y.; Hamberg, M.; Grechkin, A.N.
Stereospecific biosynthesis of (9S,13S)-10-oxo-phytoenoic acid in young maize roots
Biochim. Biophys. Acta
1851
1262-1270
2015
Zea mays
brenda
Roychowdhury, M.; Li, X.; Qi, H.; Li, W.; Sun, J.; Huang, C.; Wu, D.
Functional characterization of 9-/13-LOXs in rice and silencing their expressions to improve grain qualities
BioMed Res. Int.
2016
4275904
2016
Oryza sativa (Q9FSE5), Oryza sativa
brenda
Schiller, D.; Contreras, C.; Vogt, J.; Dunemann, F.; Defilippi, B.G.; Beaudry, R.; Schwab, W.
A dual positional specific lipoxygenase functions in the generation of flavor compounds during climacteric ripening of apple
Hortic. Res.
2
15003-15015
2015
Malus domestica (S4ULD7), Malus domestica
brenda
Zhou, G.; Ren, N.; Qi, J.; Lu, J.; Xiang, C.; Ju, H.; Cheng, J.; Lou, Y.
The 9-lipoxygenase Osr9-LOX1 interacts with the 13-lipoxygenase-mediated pathway to regulate resistance to chewing and piercing-sucking herbivores in rice
Physiol. Plant.
152
59-69
2014
Gracilaria dura
brenda
Cao, S.; Chen, H.; Zhang, C.; Tang, Y.; Liu, J.; Qi, H.
Heterologous expression and biochemical characterization of two lipoxygenases in oriental melon, Cucumis melo var. makuwa Makino
PLoS ONE
11
e0153801
2016
Cucumis melo var. makuwa (A0A125S6K7), Cucumis melo var. makuwa (A0A125S6K8)
brenda
Pilati, S.; Brazzale, D.; Guella, G.; Milli, A.; Ruberti, C.; Biasioli, F.; Zottini, M.; Moser, C.
The onset of grapevine berry ripening is characterized by reactive oxygen species accumulation and 13-lipoxygenase-derived galactolipid peroxides in the chloroplasts
Acta Hortic.
1157
105-112
2017
Vitis vinifera
-
brenda
Perry, S.C.; Horn, T.; Tourdot, B.E.; Yamaguchi, A.; Kalyanaraman, C.; Conrad, W.S.; Akinkugbe, O.; Holinstat, M.; Jacobson, M.P.; Holman, T.R.
Role of human 15-lipoxygenase-2 in the biosynthesis of the lipoxin intermediate, 5S,15S-diHpETE, implicated with the altered positional specificity of human 15-lipoxygenase-1
Biochemistry
59
4118-4130
2020
Homo sapiens (P16050), Homo sapiens
brenda
Kalms, J.; Banthiya, S.; Galemou Yoga, E.; Hamberg, M.; Holzhutter, H.G.; Kuhn, H.; Scheerer, P.
The crystal structure of Pseudomonas aeruginosa lipoxygenase Ala420Gly mutant explains the improved oxygen affinity and the altered reaction specificity
Biochim. Biophys. Acta
1862
463-473
2017
Pseudomonas aeruginosa (Q8RNT4), Pseudomonas aeruginosa
brenda
Park, J.Y.; Kim, C.H.; Choi, Y.; Park, K.M.; Chang, P.S.
Catalytic characterization of heterodimeric linoleate 13S-lipoxygenase from black soybean (Glycine max (L.) Merr.)
Enzyme Microb. Technol.
139
109595
2020
Glycine max
brenda
Ogawa, M.; Ishihara, T.; Isobe, Y.; Kato, T.; Kuba, K.; Imai, Y.; Uchino, Y.; Tsubota, K.; Arita, M.
Eosinophils promote corneal wound healing via the 12/15-lipoxygenase pathway
FASEB J.
34
12492-12501
2020
Mus musculus (P39654)
brenda
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
brenda
Wang, J.; Hu, T.; Wang, W.; Hu, H.; Wei, Q.; Wei, X.; Bao, C.
Bioinformatics analysis of the lipoxygenase gene family in radish (Raphanus sativus) and functional characterization in response to abiotic and biotic stresses
Int. J. Mol. Sci.
20
6095
2019
Raphanus sativus
brenda
Maynard, D.; Chibani, K.; Schmidtpott, S.; Seidel, T.; Spross, J.; Viehhauser, A.; Dietz, K.J.
Biochemical characterization of 13-lipoxygenases of Arabidopsis thaliana
Int. J. Mol. Sci.
22
10237
2021
Arabidopsis thaliana (P38418), Arabidopsis thaliana (Q9CAG3), Arabidopsis thaliana (Q9FNX8), Arabidopsis thaliana (Q9LNR3)
brenda
Nagasaki, T.; Schuyler, A.J.; Zhao, J.; Samovich, S.N.; Yamada, K.; Deng, Y.; Ginebaugh, S.P.; Christenson, S.A.; Woodruff, P.G.; Fahy, J.V.; Trudeau, J.B.; Stoyanovsky, D.; Ray, A.; Tyurina, Y.Y.; Kagan, V.E.; Wenzel, S.E.
15LO1 dictates glutathione redox changes in asthmatic airway epithelium to worsen type 2 inflammation
J. Clin. Invest.
132
e151685
2022
Homo sapiens (P16050)
brenda
Coppey, L.; Obrosov, A.; Shevalye, H.; Davidson, E.; Paradee, W.; Yorek, M.A.
Characterization of mice ubiquitously overexpressing human 15-lipoxygenase-1 effect of diabetes on peripheral neuropathy and treatment with menhaden oil
J. Diabetes Res.
2021
5564477
2021
Homo sapiens (P16050), Homo sapiens
brenda
Liburdi, K.; Esti, M.; Petroselli, V.; Mendler-Drienyovszki, N.; Radicetti, E.; Mancinelli, R.
Catalytic properties of lipoxygenase extracted from different varieties of Pisum sativum and Lens culinaris
J. Food Biochem.
45
e13617
2021
Lens culinaris, Pisum sativum subsp. sativum
brenda
Goftari, S.N.; Sadeghian, H.; Bahrami, A.R.; Maleki, F.; Matin, M.M.
Stylosin and some of its synthetic derivatives induce apoptosis in prostate cancer cells as 15-lipoxygenase enzyme inhibitors
Naunyn Schmiedebergs Arch. Pharmacol.
392
1491-1502
2019
Homo sapiens (P16050), Homo sapiens
brenda
Block, A.K.; Xin, Z.; Christensen, S.A.
The 13-lipoxygenase MSD2 and the omega-3 fatty acid desaturase MSD3 impact Spodoptera frugiperda resistance in Sorghum
Planta
252
62
2020
Sorghum bicolor
brenda
Menga, V.; Trono, D.
The molecular and functional characterization of the durum wheat lipoxygenase TdLOX2 suggests its role in hyperosmotic stress response
Plants (Basel)
9
1233
2020
Triticum turgidum subsp. durum (A0A7M3TWE5), Triticum turgidum subsp. durum
brenda
Qian, H.; Xia, B.; He, Y.; Lu, Z.; Bie, X.; Zhao, H.; Zhang, C.; Lu, F.
Expression, purification, and characterization of a novel acidic lipoxygenase from Myxococcus xanthus
Protein Expr. Purif.
138
13-17
2017
Myxococcus xanthus (Q1DBH9), Myxococcus xanthus, Myxococcus xanthus DK1622 (Q1DBH9)
brenda