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.
(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoic acid
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + H2O
(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoic acid
(10R)-hydroxy-(11S,12S)-epoxyeicosa-(5Z,8Z,14Z)-trienoic acid + (8R)-hydroxy-(11S,12S)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + H2O
-
-
the former being a isomer of hepoxilin A3, ration of products is 2:1
?
(13R)-hydroperoxylinolenic acid
13-ketolinolenic acid + threo-11-hydroxy-(12R,13R)-epoxy-(9Z,15Z)-octadecadienoic acid + erythro-11-hydroxy-(12R,13R)-epoxy-(9Z,15Z)-octadecadienoic acid
the G316A mutant converts (13R)-hydroperoxylinolenic acid to 13-ketolinolenic acid (with an apparent Km of 0.01 mM) and to epoxyalcohols viz. erythro- and threo-11-hydroxy-(12R,13R)-epoxy-(9Z,15Z)-octadecadienoic acids and one of the corresponding cis-epoxides as major products
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
(13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoic acid
(12,13S)-epoxy-(9Z,11,15Z)-octadecatrienoic acid + H2O
-
-
12-oxo-13-hydroxy-(9Z,15Z)-octadecadienoic acid + 12-oxo-(10,15Z)-phytodienoic acid, formed by spontaneous chemical or enzyme-catalyzed cyclization
?
(13S)-hydroperoxy-(9Z,11Z,15Z)-octadecatrienoic acid
(12,13S)-epoxy-(9Z,11Z,15Z)-octadecatrienoic acid + H2O
by AOS1
-
-
?
(13S)-hydroperoxyoctadecadienoic acid
13-hydroxy-12-oxo-9(Z)-octadecenoic acid + 12-oxo-10-phytoenoic acid
-
-
13-hydroxy-12-oxo-(9Z)-octadecenoic acid is the major product
-
?
(13S)-hydroperoxyoctadecatrienoic acid
13-hydroxy-12-oxo-(9Z,15Z)-octadecadienoic acid + 12-oxo-(10Z,15Z)-phytodienoic acid
-
-
OsAOS1 produces a 1:1 racemic mixture of cis-(+)/cis-(-)-12-oxo-(10Z,15Z)-phytodienoic acid via non-enzymatic cyclization of 12,13-epoxy-9,11,15-octadecatrienoic acid, an unstable allene oxide
-
?
(13S,9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
?
-
is converted to an allene oxide
-
-
?
(15S)-hydroperoxyeicosatetraenoic acid
(15S)-hydroxy-11,12-epoxyeicosatrienoic acid + H2O
-
-
-
-
?
(5Z,8Z,11E,13Z,15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoic acid
14,15-hepoxilin A3 + 14,15-hepoxilin B3 + H2O
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoic acid
(8E)-10-oxodecenoic acid + 1-octen-3-ol + (2Z)-octen-1-ol
the catalase-related hemoprotein reacts rapidly and specifically with linoleate 10S-hydroperoxide with a hydroperoxide lyase activity specific for the 10S-hydroperoxy enantiomer
in a 3:1 ratio, strict enzymatic control in formation of the 3R alcohol configuration with 99% enantiomeric excess
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
(8R)-hydroperoxyeicosatetraenoic acid
?
(8R)-hydroperoxylinoleic acid + H2O
(5S,8R)-dihydroxylinoleic acid
-
-
-
-
?
(8R)-hydroperoxylinoleic acid + H2O
(8R,11S)-dihydroxylinoleic acid
-
-
-
-
?
(8R)-hydroxyeicosatetraenoic acid
(8R)-hydroxy-(9R,10R)-trans-epoxy-eicosa-(5Z,11Z,14Z)-trienoic acid
-
the native, unmodified enzyme shows no activity with (8R)-hydroxyeicosatetraenoic acid, but the oxidized enzyme epoxidizes the substrate analogue stereospecifically on the 9,10-double bond to form (8R)-hydroxy-(9R,10R)-trans-epoxy-eicosa-(5Z,11Z,14Z)-trienoic acid as the predominant product, via Compound I (FeV=O) intermediate
erythro and threo diastereomers of (8R)-hydroxy-9,10-trans-epoxy-eicosa-5Z,11Z,14Z-trienoate
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9R,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
recombinant FOXB_01332 oxidizes 18:2n-6 to (9S)-hydroperoxy-10(E),12(Z)-octadecadienoic acid by hydrogen abstraction and antarafacial insertion of molecular oxygen and sequentially to an allene oxide, (90S)-(10)-epoxy-10,12(Z)-octadecadienoic acid, which gives nonenzymatic hydrolysis products alpha- and gamma-ketols
-
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
10-oxo-(9R)-hydroxy-cis-12-octadecadienoic acid + H2O
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
9-oxononanoic acid + (3Z)-nonenal
-
-
-
-
?
(9S)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
(9S,10)-epoxy-(10Z,12Z,15Z)-octadecatrienoic acid + H2O
-
-
-
?
(9S)-hydroperoxyoctadecadienoic acid
?
-
-
-
-
?
(9S)-hydroperoxyoctadecatrienoic acid
?
-
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + H2O + ?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
(9Z,11E,13R)-13-hydroperoxyoctadeca-9,11-dienoic acid
11-hydroxy-12(13)-epoxy-octadecadienoic acid + 9-hydroxy-12(13)-epoxy-octadecadienoic acid + H2O
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
?
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
13-hydroperoxy-(10E,12Z)-octadecadienoic acid
11-hydroxy-12(13)-epoxy-octadecadienoic acid + 9-hydroxy-12(13)-epoxy-octadecadienoic acid + H2O
13-hydroperoxy-9,11,15-octadecatrienoic acid
?
-
-
-
-
?
13-hydroperoxy-9,11-octadecadienoic acid
(10E,12Z)-12-[(3S)-3-methyl-3-propyloxiran-2-ylidene]dodec-10-enoic acid + H2O
-
wild-type AOS activity
-
-
?
13-hydroperoxy-9,11-octadecadienoic acid
(10E,12Z)-13-[(2-hydroxypentan-2-yl)oxy]trideca-10,12-dienoic acid + H2O
-
activity of AOS mutant F137L
-
-
?
13-hydroperoxy-9,11-octadecadienoic acid
?
-
-
-
-
?
13-hydroperoxylinoleic acid
(Z)-3-hexanal + 12-oxododecenoic acid
-
-
-
-
?
13-hydroperoxylinoleic acid
?
-
-
-
-
?
13-hydroperoxylinolenic acid
12-oxo-cis-10,15-phytodienoic acid + (12Z,15Z)-9-hydroxy-10-oxooctadeca-12,15-dienoic acid + H2O
-
-
the latter is a minor product of approximately 5%
?
9-hydroperoxylinolenic acid
13-hydroxy-10-oxo-cis-15-trans-11-octadecadienoic acid + H2O
-
-
-
?
alpha-linolenic acid
(E,Z)-3,6-nonadienal + 9-oxononanoic acid
-
cleavage of 9-hydroperoxy fatty acid
-
-
?
heptadecatrienoic acid
12-hydroperoxyheptadecatrienoic acid + (8Z,10S,11Z,14Z)-10-hydroperoxyheptadeca-8,11,14-trienoic acid
the G316A mutant transforms 17:3n-3 to both 12-hydroperoxyheptadecatrienoic acid (about 93%) and 10-hydroperoxyheptadecatrienoic acid (7%)
-
-
?
linoleate hydroperoxide + H2O
9,12,13-trihydroxy-trans-10-octadecenoic acid + 9,10,13-trihydroxy-trans-11-octadecenoic acid
-
-
-
-
?
linoleic acid
(Z)-3-nonenal + 9-oxononanoic acid
-
cleavage of 9-hydroperoxy fatty acid
-
-
?
linoleic acid
?
Mn-LO G316A metabolizeS 18:2n-6 to (11S)-hydroperoxyoctadecadienoic acid and (13R)-hydroperoxyoctadecadienoic acid in approximately the same relative amounts as the native enzyme, and (13R)-hydroperoxyoctadecadienoic acid accumulates as the end product
-
-
?
linolenic acid
(13R)-hydroperoxyoctadecatrienoic acid + (11S)-hydroperoxyoctadecatrienoic acid
Mn-LO G316A metabolizes 18:3n-3 to (13R)-hydroperoxyoctadecatrienoic acid and (11S)-hydroperoxyoctadecatrienoic acid
-
-
?
linolic acid hydroperoxide + H2O
9,12,13-trihydroxy-trans-10-octadecenoic acid + 9,10,13-trihydroxy-trans-11-octadecenoic acid
-
-
-
?
additional information
?
-
(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoic acid
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + H2O
-
intramolecular oxygenation with retention of the configuration of the carbon atom hydroxylated
-
?
(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoic acid
(8R)-hydroxy-(11R,12R)-epoxyeicosa-(5Z,9E,14Z)-trienoic acid + H2O
-
poor substrate
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
substrate listed without specification of steroisomer used
products are 10,13-dihydroxyoctadec-11-enoic acid + 12,13-dihydroxyoctadec-9-enoic acid + trace amounts of 9,12-dihydroxyoctadec-10-enoic acid
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
(S)-hydroperoxy-(9Z,11E)-octadecadienoic acid is a poor substrate
products are: (11R,12R)-epoxy-(13S)-hydroxy-(9Z)-octadecenoic acid + (9S,10R)-epoxy-(13S)-hydroxy-(11E)-octadecenoic acid
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
products are: 13-hydroxy-12-oxo-cis-9-octadecenoic acid + small amounts of the gamma ketol
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12S,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
spontaneous hydrolysis to 12-keto-13-hydroxy-(9Z)-octadecenoic acid (72% 13(R) and 28% 13(S))
?
(5Z,8Z,11E,13Z,15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoic acid
14,15-hepoxilin A3 + 14,15-hepoxilin B3 + H2O
-
high stereoselectivity, not with 15(R)-substrate
mixture of both products
?
(5Z,8Z,11E,13Z,15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoic acid
14,15-hepoxilin A3 + 14,15-hepoxilin B3 + H2O
-
poor substrate
-
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
-
-
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
-
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
-
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
stereospecific elimination of the pro-S hydrogen from C-7 and intramolecular suprafacial insertion of oxygen at C-7 with retention of the absolute configuration at C-7
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
-
-
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
stereospecific elimination of the pro-S hydrogen from C-7 and intramolecular suprafacial insertion of oxygen at C-7 with retention of the absolute configuration at C-7
-
?
(8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
(7S,8S)-dihydroxy-(9Z,12Z)-octadecadienoic acid + H2O
-
poor substrate
-
-
?
(8R)-hydroperoxyeicosatetraenoic acid
?
-
the substrate is converted to an unstable allene oxide product via the FeIV-OH intermediate, Compound II, the native enzyme shows a strong preference for its natural substrate
-
-
?
(8R)-hydroperoxyeicosatetraenoic acid
?
-
the substrate is converted to an unstable allene oxide product via the FeIV-OH intermediate, Compound II
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9R,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid
-
an unstable allene oxide
-
?
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9R,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid
-
an unstable allene oxide
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
recombinant FOXB_01332 oxidizes 18:2n-6 to (9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid by hydrogen abstraction and antarafacial insertion of molecular oxygen and sequentially to an allene oxide, (9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid, which gives nonenzymatic hydrolysis products alpha- and gamma-ketols
-
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
recombinant FOXB_01332 oxidizes 18:2n-6 to (9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid by hydrogen abstraction and antarafacial insertion of molecular oxygen and sequentially to an allene oxide, (9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid, which gives nonenzymatic hydrolysis products alpha- and gamma-ketols
-
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
10-oxo-(9R)-hydroxy-cis-12-octadecadienoic acid + H2O
-
-
9-hydroxy-10-oxo,cis-12-octadecenoic acid and 13-hydroxy-10-oxo-trans-11-octadecenoic acid in the ratio 2:1
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
10-oxo-(9R)-hydroxy-cis-12-octadecadienoic acid + H2O
-
(S)-hydroperoxy-(10E,12Z)-octadecadienoic acid is a poor substrate
products: (10R,11R)-epoxy-(9S)-hydroxy-(12Z)-octadecenoic acid + (12R,13S)-epoxy-(9S)-hydroxy-(10E)-octadecenoic acid
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
10-oxo-(9R)-hydroxy-cis-12-octadecadienoic acid + H2O
-
-
-
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
10-oxo-(9R)-hydroxy-cis-12-octadecadienoic acid + H2O
-
-
-
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
10-oxo-(9R)-hydroxy-cis-12-octadecadienoic acid + H2O
-
-
in presence of linoleate the product is (9R)-linoleoyloxy-10-oxo-cis-12-octadecenoic acid
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + H2O + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + H2O + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
?
-
the divinyl ether synthase enzyme mutant E292G shows allene oxide synthase activity, producing the typical allene oxide synthase product alpha-ketol and 12-oxo-10,15-phytodienoic acid, and lacks divinyl ether synthase activity in contrast to the wild-type divinyl ether synthase CYP74B16
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
?
-
the divinyl ether synthase enzyme mutant V379F shows allene oxide synthase activity, producing the typical allene oxide synthase product alpha-ketol, and lacks divinyl ether synthase activity in contrast to the wild-type divinyl ether synthase CYP74D3
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13R)-13-hydroperoxyoctadeca-9,11-dienoic acid
11-hydroxy-12(13)-epoxy-octadecadienoic acid + 9-hydroxy-12(13)-epoxy-octadecadienoic acid + H2O
-
-
-
?
(9Z,11E,13R)-13-hydroperoxyoctadeca-9,11-dienoic acid
11-hydroxy-12(13)-epoxy-octadecadienoic acid + 9-hydroxy-12(13)-epoxy-octadecadienoic acid + H2O
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
13-HPOD
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
?
-
the divinyl ether synthase enzyme mutant E292G shows allene oxide synthase activity, producing the typical allene oxide synthase product alpha-ketol and 12-oxo-10,15-phytodienoic acid, and lacks divinyl ether synthase activity in contrast to the wild-type divinyl ether synthase CYP74B16
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
?
-
the divinyl ether synthase enzyme mutant V379F shows allene oxide synthase activity, producing the typical allene oxide synthase product alpha-ketol, and lacks divinyl ether synthase activity in contrast to the wild-type divinyl ether synthase CYP74D3
-
-
?
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
-
-
-
?
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
-
-
-
?
13-hydroperoxy-(10E,12Z)-octadecadienoic acid
11-hydroxy-12(13)-epoxy-octadecadienoic acid + 9-hydroxy-12(13)-epoxy-octadecadienoic acid + H2O
-
-
-
?
13-hydroperoxy-(10E,12Z)-octadecadienoic acid
11-hydroxy-12(13)-epoxy-octadecadienoic acid + 9-hydroxy-12(13)-epoxy-octadecadienoic acid + H2O
-
-
-
?
additional information
?
-
the enzyme catalyzes the first specific reaction in the formation of 12-oxophytodienoic acid, a signaling compound with multiple functions that is also the immediate precursor of jasmonic acid
-
-
?
additional information
?
-
-
the enzyme catalyzes the first specific reaction in the formation of 12-oxophytodienoic acid, a signaling compound with multiple functions that is also the immediate precursor of jasmonic acid
-
-
?
additional information
?
-
galactoplid bound hydroperoxides are substrates for CYP74 members
-
-
?
additional information
?
-
-
two hydroperoxide isomerases in Aspergillus clavatus acting on hydroperoxylinoleic acid: the 5,8-linoleate diol synthase exhibiting 5,8-hydroperoxide isomerase activity, and the 8, 11-linoleate diol synthase exhibiting 8,11-hydroperoxide isomerase activity, overview
-
-
?
additional information
?
-
Asn964 may facilitate homolytic cleavage of the dioxygen bond of (9R)-hydroperoxy-10(E),12(Z)-octadecadienoic acid with formation of compound II. No activity with 18:2n-6
-
-
?
additional information
?
-
-
Asn964 may facilitate homolytic cleavage of the dioxygen bond of (9R)-hydroperoxy-10(E),12(Z)-octadecadienoic acid with formation of compound II. No activity with 18:2n-6
-
-
?
additional information
?
-
Asn964 may facilitate homolytic cleavage of the dioxygen bond of (9R)-hydroperoxy-10(E),12(Z)-octadecadienoic acid with formation of compound II. No activity with 18:2n-6
-
-
?
additional information
?
-
the recombinant enzyme (encoded by gene CYP74B24) produces (Z)-3-hexenal from 13-HPOT with the optimal pH 6.0 in vitro
-
-
?
additional information
?
-
-
the recombinant enzyme (encoded by gene CYP74B24) produces (Z)-3-hexenal from 13-HPOT with the optimal pH 6.0 in vitro
-
-
?
additional information
?
-
-
cleavage of 9-hydroperoxy fatty acids or 13-hydroperoxy fatty acids by a hydroperoxide lyase results in formation of aldehydes (Z)-3-nonenal/(E,Z)-3,6-nonadienal or (Z)-3-hexanal, and omega-oxo fatty acid 9-oxo-nonanoic acid or 12-oxo-dodecenoic acid, respectively
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specificities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview. No activity with (9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specificities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specificities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
mechanism of formation of fatty acid diepoxy ketone, overview. No reaction with 9R- and 9S-hydroperoxy-9,11-octadecadienoates. Peroxidase assay monitoring the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonic acid (ABTS), enzyme Fg-cat exhibits robust activity (kcat 550 s/1) using the 13S-hydroperoxy-C18 fatty acids as the oxidizing co-substrate
-
-
?
additional information
?
-
-
mechanism of formation of fatty acid diepoxy ketone, overview. No reaction with 9R- and 9S-hydroperoxy-9,11-octadecadienoates. Peroxidase assay monitoring the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonic acid (ABTS), enzyme Fg-cat exhibits robust activity (kcat 550 s/1) using the 13S-hydroperoxy-C18 fatty acids as the oxidizing co-substrate
-
-
?
additional information
?
-
mechanism of formation of fatty acid diepoxy ketone, overview. No reaction with 9R- and 9S-hydroperoxy-9,11-octadecadienoates. Peroxidase assay monitoring the oxidation of 2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonic acid (ABTS), enzyme Fg-cat exhibits robust activity (kcat 550 s/1) using the 13S-hydroperoxy-C18 fatty acids as the oxidizing co-substrate
-
-
?
additional information
?
-
FOXB_01332 is a linoleate 9-dioxygenase with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein
-
-
?
additional information
?
-
-
FOXB_01332 is a linoleate 9-dioxygenase with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein
-
-
?
additional information
?
-
(9S)-dioxygenase-allene oxide synthase converts 9S-hydroperoxyoctadecadienoic acid to alpha- and gamma-ketols, likely formed by hydrolysis of (9S,10)-(10)-epoxy-(10Z,12Z)-octadecadienoic acid, along with small amounts of epoxy alcohols. The (9R)-hydroperoxyoctadecadienoic acid preparation contains a few percent (9S)-hydroperoxyoctadecadienoic acid, and only the latter is apparently transformed to an alpha-ketol by (9S)-dioxygenase-allene oxide synthase. (13S)-hydroperoxyoctadecadienoic acid, (13S)-hydroxy-(10E,12Z,15Z)-octadecatrienoicacid, (13R)-hydroperoxyoctadecadienoic acid, and (13R)-hydroxy-(10E,12Z,15Z)-octadecatrienoicacid are not transformed to detectable amounts of allene oxides/alpha-ketols, but variable amounts of epoxy alcohols accumulate, mass spectrometric analysis of products, substrate specificity, overview
-
-
?
additional information
?
-
-
(9S)-dioxygenase-allene oxide synthase converts 9S-hydroperoxyoctadecadienoic acid to alpha- and gamma-ketols, likely formed by hydrolysis of (9S,10)-(10)-epoxy-(10Z,12Z)-octadecadienoic acid, along with small amounts of epoxy alcohols. The (9R)-hydroperoxyoctadecadienoic acid preparation contains a few percent (9S)-hydroperoxyoctadecadienoic acid, and only the latter is apparently transformed to an alpha-ketol by (9S)-dioxygenase-allene oxide synthase. (13S)-hydroperoxyoctadecadienoic acid, (13S)-hydroxy-(10E,12Z,15Z)-octadecatrienoicacid, (13R)-hydroperoxyoctadecadienoic acid, and (13R)-hydroxy-(10E,12Z,15Z)-octadecatrienoicacid are not transformed to detectable amounts of allene oxides/alpha-ketols, but variable amounts of epoxy alcohols accumulate, mass spectrometric analysis of products, substrate specificity, overview
-
-
?
additional information
?
-
FOXB_01332 is a linoleate 9-dioxygenase with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein
-
-
?
additional information
?
-
(9S)-dioxygenase-allene oxide synthase converts 9S-hydroperoxyoctadecadienoic acid to alpha- and gamma-ketols, likely formed by hydrolysis of (9S,10)-(10)-epoxy-(10Z,12Z)-octadecadienoic acid, along with small amounts of epoxy alcohols. The (9R)-hydroperoxyoctadecadienoic acid preparation contains a few percent (9S)-hydroperoxyoctadecadienoic acid, and only the latter is apparently transformed to an alpha-ketol by (9S)-dioxygenase-allene oxide synthase. (13S)-hydroperoxyoctadecadienoic acid, (13S)-hydroxy-(10E,12Z,15Z)-octadecatrienoicacid, (13R)-hydroperoxyoctadecadienoic acid, and (13R)-hydroxy-(10E,12Z,15Z)-octadecatrienoicacid are not transformed to detectable amounts of allene oxides/alpha-ketols, but variable amounts of epoxy alcohols accumulate, mass spectrometric analysis of products, substrate specificity, overview
-
-
?
additional information
?
-
-
overview on substrates, configurations and mechanism
-
-
?
additional information
?
-
catalytic properties of Mn-LO and the G316A mutant with heptadecatrienic acid, 18:2n-6, octadecatrienoic acid, and nonadecatrienoic acid as substrates: increasing the fatty acid chain length from C17 to C19 shifts the oxygenation by Mn-LO from the n-6 toward the n-8 carbon. The G316A mutant increases the oxygenation at the n-8 carbon of 17:3n-3 and at the n-10 carbon of the C17 and C18 fatty acids (from 12% to 711%). The most striking effect of the G316A mutant is a 2fold, 7fold, and 15fold increase in transformation of the n-6 hydroperoxides of 19:3n-3, 18:3n-3, and 17:3n-3, respectively, to keto fatty acids and epoxyalcohols. The n-3 double bond is essential. Both oxygen atoms are retained in the epoxyalcohols. (R)-Hydroperoxides at n-6 of C17:3, 18:3, and 19:3 are transformed 5times faster than (S)-stereoisomers
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
-
overview on substrates, configurations and mechanism
-
-
?
additional information
?
-
-
CYP74 enzymes use their fatty acid hydroperoxide substrate to activate the enzyme and substrate in one and the same step
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
-
the enzyme cleaves 13(S)-hydroperoxy-C18 fatty acids into C6-aldehyde and C12-oxo-acid
-
-
?
additional information
?
-
-
the enzyme cleaves 13(S)-hydroperoxy-C18 fatty acids into C6-aldehyde and C12-oxo-acid. GC-MS product analysis
-
-
?
additional information
?
-
-
the enzyme cleaves 13(S)-hydroperoxy-C18 fatty acids into C6-aldehyde and C12-oxo-acid
-
-
?
additional information
?
-
-
the enzyme cleaves 13(S)-hydroperoxy-C18 fatty acids into C6-aldehyde and C12-oxo-acid. GC-MS product analysis
-
-
?
additional information
?
-
the enzyme mainly acts as an oleate or linoleate dioxygenase, albeit with alpha-linolenic acid very competitive at low substrate concentrations, substrate specificity and kinetics, overview
-
-
?
additional information
?
-
according to their specificity, HPLs can act on the 9- or 13-hydroperoxides of linoleic and linolenic acids (hydroperoxyoctadecadienoic acid (HPOD) and hydroperoxyoctadecatrienoic acid (HPOT)) and catalyze the cleavage of these hydroperoxides into C6- or C9-aldehydes and the C12- or C9-oxo-acids, respectively
-
-
?
additional information
?
-
the recombinant 13-HPL enzyme is assayed as biocatalyst to produce C6-aldehydes. Bioconversion of 13-hydroperoxides of linoleic and linolenic acids by recombinant enzyme with or without chloroplast targeting signal sequence, reaction products are identified and quantified using gas chromatography and mass spectrometry. Recombinant HPL enzyme with targeting sequence allows production of 5.61 mM hexanal and 4.39 mM (Z)-3-hexenal, corresponding to high conversion yields of 93.5% and 73%, respectively. The HPL enzyme without targeting sequence fails to obtain greater quantities of hexanal or (Z)-3-hexenal. No undesirable products are formed, and no isomerization of (Z)-3-hexenal in (E)-2-hexenal occurs
-
-
?
additional information
?
-
-
cleavage of 9-hydroperoxy fatty acids in vivo, AOS enzymes also convert hydroperoxy fatty acids to aldehydes via an HPL-like activity
-
-
?
additional information
?
-
-
OsHPL3 possesses intrinsic hydroperoxide lyase activity hydrolyzing hydroperoxylinolenic acid to produce green leaf volatiles, it catabolizes 9/13-hydroperoxylinoleic acid to form (Z)-3-hexenal
-
-
?
additional information
?
-
-
allene oxide synthase converts fatty acid hydroperoxides into unstable fatty acid epoxides (allene oxides). OsAOS1 exhibits dual positional substrate specificity and prefers 13-positional isomeric to 9-positional isomeric substrates in vitro. OsAOS1 converts (9S)-hydroperoxyoctadecadienoic acid or (9S)-hydroperoxyoctadecatrienoic acid into the corresponding unstable allene oxides, which are non-enzymatically transformed into a 9alpha-ketol as the major product, and 13gamma-ketols and cyclopentenone derivatives as minor products
-
-
?
additional information
?
-
allene oxide synthase is a key cytochrome P450 enzyme in the oxylipin pathway leading to allene oxide synthase-derived jasmonates
-
-
?
additional information
?
-
-
allene oxide synthase is a key cytochrome P450 enzyme in the oxylipin pathway leading to allene oxide synthase-derived jasmonates
-
-
?
additional information
?
-
-
13-HPL and 9-HPL activities on oxylipins, traumatin derivatives, in different plant organs, overview
-
-
?
additional information
?
-
-
the native enzyme is completely unreactive with polyunsaturated fatty acids or their hydroxylated analogues. Mass spectrometric product analysis, overview
-
-
?
additional information
?
-
-
in case of hydroperoxide lyases the homolytic isomerization of fatty acid hydroperoxides leads to a short-lived hemiacetal, which spontaneously disintegrates into (Z)-3-hexenal and (9Z)-12-oxo-9-dodecenoic acid
-
-
?
additional information
?
-
-
overview on substrates, configurations and mechanism
-
-
?
additional information
?
-
analysis of hexanal, (Z)-3-hexenal, (E)-2-hexenal, and (Z)-3-hexen-1-ol levels by gas chromatography
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
no activity with (9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview. No activity with (9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
(8R)-hydroperoxyeicosatetraenoic acid
?
-
the substrate is converted to an unstable allene oxide product via the FeIV-OH intermediate, Compound II, the native enzyme shows a strong preference for its natural substrate
-
-
?
(8R)-hydroperoxylinoleic acid + H2O
(5S,8R)-dihydroxylinoleic acid
-
-
-
-
?
(8R)-hydroperoxylinoleic acid + H2O
(8R,11S)-dihydroxylinoleic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9R,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + H2O + ?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
13-hydroperoxy-9,11-octadecadienoic acid
(10E,12Z)-12-[(3S)-3-methyl-3-propyloxiran-2-ylidene]dodec-10-enoic acid + H2O
-
wild-type AOS activity
-
-
?
13-hydroperoxy-9,11-octadecadienoic acid
(10E,12Z)-13-[(2-hydroxypentan-2-yl)oxy]trideca-10,12-dienoic acid + H2O
-
activity of AOS mutant F137L
-
-
?
13-hydroperoxylinoleic acid
(Z)-3-hexanal + 12-oxododecenoic acid
-
-
-
-
?
alpha-linolenic acid
(E,Z)-3,6-nonadienal + 9-oxononanoic acid
-
cleavage of 9-hydroperoxy fatty acid
-
-
?
linoleic acid
(Z)-3-nonenal + 9-oxononanoic acid
-
cleavage of 9-hydroperoxy fatty acid
-
-
?
additional information
?
-
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(13S)-hydroperoxy-(9Z,11E)-octadecadienoic acid
(12,13S)-oxido-(9Z,11)-octadecadienoic acid + H2O
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R)-hydroperoxy-(10E,12Z,15Z)-octadecatrienoic acid
9-hydroxy-10-oxo-(12Z,15Z)-octadecadienoic acid
-
-
-
-
?
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9R,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid
-
an unstable allene oxide
-
?
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9R,10)-10-epoxy-(10Z,12Z)-octadecadienoic acid
-
an unstable allene oxide
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
recombinant FOXB_01332 oxidizes 18:2n-6 to (9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid by hydrogen abstraction and antarafacial insertion of molecular oxygen and sequentially to an allene oxide, (9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid, which gives nonenzymatic hydrolysis products alpha- and gamma-ketols
-
-
?
(9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid
(9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid + H2O
recombinant FOXB_01332 oxidizes 18:2n-6 to (9S)-hydroperoxy-(10E,12Z)-octadecadienoic acid by hydrogen abstraction and antarafacial insertion of molecular oxygen and sequentially to an allene oxide, (9S,10)-epoxy-(10Z,12Z)-octadecadienoic acid, which gives nonenzymatic hydrolysis products alpha- and gamma-ketols
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + H2O + ?
-
-
-
?
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
(9S,10S,11S,12Z)-9,10-epoxy-11-hydroxy-12-octadecenoic acid + 9-hydroxy-10-oxo-12-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + H2O + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
9-hydroxynonanoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
11-hydroxy-12,13-epoxy-9-octadecenoic acid + 9-hydroxy-12,13-epoxy-10-octadecenoic acid + (9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
hexanal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(9Z)-12-hydroxy-9-dodecenoic acid + (10E)-12-hydroxy-10-dodecenoic acid + ?
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
?
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
(Z)-3-hexenal + 12-oxo-9-dodecenoic acid
-
-
-
-
?
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
-
-
-
?
(9Z,11E,15Z)-(13S)-hydroperoxyoctadeca-9,11,15-trienoate
(9Z,15Z)-(13S)-12,13-epoxyoctadeca-9,11,15-trienoate + H2O
-
-
-
?
additional information
?
-
the enzyme catalyzes the first specific reaction in the formation of 12-oxophytodienoic acid, a signaling compound with multiple functions that is also the immediate precursor of jasmonic acid
-
-
?
additional information
?
-
-
the enzyme catalyzes the first specific reaction in the formation of 12-oxophytodienoic acid, a signaling compound with multiple functions that is also the immediate precursor of jasmonic acid
-
-
?
additional information
?
-
galactoplid bound hydroperoxides are substrates for CYP74 members
-
-
?
additional information
?
-
-
two hydroperoxide isomerases in Aspergillus clavatus acting on hydroperoxylinoleic acid: the 5,8-linoleate diol synthase exhibiting 5,8-hydroperoxide isomerase activity, and the 8, 11-linoleate diol synthase exhibiting 8,11-hydroperoxide isomerase activity, overview
-
-
?
additional information
?
-
-
cleavage of 9-hydroperoxy fatty acids or 13-hydroperoxy fatty acids by a hydroperoxide lyase results in formation of aldehydes (Z)-3-nonenal/(E,Z)-3,6-nonadienal or (Z)-3-hexanal, and omega-oxo fatty acid 9-oxo-nonanoic acid or 12-oxo-dodecenoic acid, respectively
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specificities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specificities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specificities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
FOXB_01332 is a linoleate 9-dioxygenase with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein
-
-
?
additional information
?
-
-
FOXB_01332 is a linoleate 9-dioxygenase with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein
-
-
?
additional information
?
-
FOXB_01332 is a linoleate 9-dioxygenase with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
additional information
?
-
-
the enzyme cleaves 13(S)-hydroperoxy-C18 fatty acids into C6-aldehyde and C12-oxo-acid
-
-
?
additional information
?
-
-
the enzyme cleaves 13(S)-hydroperoxy-C18 fatty acids into C6-aldehyde and C12-oxo-acid
-
-
?
additional information
?
-
according to their specificity, HPLs can act on the 9- or 13-hydroperoxides of linoleic and linolenic acids (hydroperoxyoctadecadienoic acid (HPOD) and hydroperoxyoctadecatrienoic acid (HPOT)) and catalyze the cleavage of these hydroperoxides into C6- or C9-aldehydes and the C12- or C9-oxo-acids, respectively
-
-
?
additional information
?
-
-
cleavage of 9-hydroperoxy fatty acids in vivo, AOS enzymes also convert hydroperoxy fatty acids to aldehydes via an HPL-like activity
-
-
?
additional information
?
-
-
OsHPL3 possesses intrinsic hydroperoxide lyase activity hydrolyzing hydroperoxylinolenic acid to produce green leaf volatiles, it catabolizes 9/13-hydroperoxylinoleic acid to form (Z)-3-hexenal
-
-
?
additional information
?
-
allene oxide synthase is a key cytochrome P450 enzyme in the oxylipin pathway leading to allene oxide synthase-derived jasmonates
-
-
?
additional information
?
-
-
allene oxide synthase is a key cytochrome P450 enzyme in the oxylipin pathway leading to allene oxide synthase-derived jasmonates
-
-
?
additional information
?
-
-
13-HPL and 9-HPL activities on oxylipins, traumatin derivatives, in different plant organs, overview
-
-
?
additional information
?
-
reaction products are identified and quantified using HPLC chromatography and mass spectrometry, product specifities, overview
-
-
?
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.
494.5
(13S)-hydroperoxyoctadecadienoic acid
-
pH 7.5, 22°C
537.8
(13S)-hydroperoxyoctadecatrienoic acid
-
pH 7.5, 22°C
44.9
(9S)-hydroperoxyoctadecadienoic acid
-
pH 7.5, 22°C
17.5
(9S)-hydroperoxyoctadecatrienoic acid
-
pH 7.5, 22°C
228.6 - 1115.9
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
173.8 - 867.7
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
17.89 - 1587.5
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
187.1 - 997
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
228.6
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
455.3
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
571.4
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant mutant L97F/TCFNSF enzyme
676.4
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
732.4
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant mutant L93F/G283A enzyme
773.3
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
949.6
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant mutant L98F/A287G enzyme
1115.9
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
173.8
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
337.6
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
356.1
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant mutant L98F/A287G enzyme
375.4
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
550
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant mutant L97F/TCFNSF enzyme
600
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
619.8
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant mutant L93F/G283A enzyme
867.7
(9S,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
17.89
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.5, 25°C, recombinant truncated enzyme
26.38
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.5, 25°C, recombinant full-length enzyme
42
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.5, 25°C, recombinant full-length enzyme, with 2.5% glycine w/v
46.9
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.5, 25°C, recombinant truncated enzyme, with 2.5% glycine w/v
73.2
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.5, 25°C, recombinant truncated enzyme, with 0.5 M NaCl
133.9
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.5, 25°C, recombinant full-length enzyme, with 0.5 M NaCl
290
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
471.4
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant mutant L97F/TCFNSF enzyme
596.4
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
712.7
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant mutant L93F/G283A enzyme
752.4
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
913.3
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
1011.6
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
1587.5
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid
pH 7.0, 23°C, recombinant mutant L98F/A287G enzyme
187.1
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant mutant L97F/TCFNSF enzyme
377.2
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
402.62
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.5, 25°C, recombinant truncated enzyme
530.9
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
564.95
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.5, 25°C, recombinant full-length enzyme
579
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.5, 25°C, recombinant full-length enzyme, with 0.5 M NaCl
587.4
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.5, 25°C, recombinant full-length enzyme, with 2.5% glycine w/v
701.6
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.5, 25°C, recombinant truncated enzyme, with 0.5 M NaCl
768.9
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant wild-type enzyme
829.1
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant mutant L93F/G283A enzyme
843.3
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.5, 25°C, recombinant truncated enzyme, with 2.5% glycine w/v
997
(9Z,11E,13S,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid
pH 7.0, 23°C, recombinant mutant L98F/A287G enzyme
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.
evolution
-
phylogenetic analysis and sequence comparisons of 5,8-linoleate diol synthase, overview
evolution
-
allene oxide synthases, like hydroperoxide lyases and divinyl ether synthases belong to the CYP74 family of cytochrome P450 enzymes. These enzymes rearrange fatty acid hydroperoxides differently, sharing an epoxyallylic radical as a common intermediate
evolution
-
AOS is a non-classical cytochrome P450, which, like other CYP74 enzymes, does not require molecular oxygen and NADPH-dependent P450 reductase
evolution
FOXB_01332 is a linoleate 9-DOX with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein. The conserved Tyr-(His/Arg)-Trp-His motif contains a Phe instead of the catalytic Tyr residue, which is oxidized by the heme to a radical that performs the hydrogen abstraction of LDS and COX, the replacement of Phe 416 with Trp does not affect the product profile of FOXB_01332
evolution
-
phylogenetic relationship of pearl millet PgAOS1 and other known allene oxide synthases, overview
evolution
the fungal allene oxide synthases belongs to the CYP74 family
evolution
hydroperoxide lyases are classified in the cytochrome P450 family and more particularly in the two subfamilies CYP74B (13-HPL) and CYP74C (9-HPL and 9/13-HPL)
evolution
hydroxyperoxide lyases belong to the CYP74C subfamily of fatty acid hydroperoxide transforming enzymes, unrooted phylogenetic tree of CYP74 family with special emphasis to CYP74C subfamily, overview
evolution
hydroxyperoxide lyases belong to the CYP74C subfamily of fatty acid hydroperoxide transforming enzymes, unrooted phylogenetic tree of CYP74 family with special emphasis to CYP74C subfamily, overview
evolution
hydroxyperoxide lyases belong to the CYP74C subfamily of fatty acid hydroperoxide transforming enzymes, unrooted phylogenetic tree of CYP74 family with special emphasis to CYP74C subfamily, overview
evolution
hydroxyperoxide lyases belong to the CYP74C subfamily of fatty acid hydroperoxide transforming enzymes, unrooted phylogenetic tree of CYP74 family with special emphasis to CYP74C subfamily, overview
evolution
hydroxyperoxide lyases belong to the CYP74C subfamily of fatty acid hydroperoxide transforming enzymes, unrooted phylogenetic tree of CYP74 family with special emphasis to CYP74C subfamily, overview
evolution
-
FOXB_01332 is a linoleate 9-DOX with homology to animal heme peroxidases and a 9-dioxygenase-allene oxide synthase fusion protein. The conserved Tyr-(His/Arg)-Trp-His motif contains a Phe instead of the catalytic Tyr residue, which is oxidized by the heme to a radical that performs the hydrogen abstraction of LDS and COX, the replacement of Phe 416 with Trp does not affect the product profile of FOXB_01332
-
evolution
-
the fungal allene oxide synthases belongs to the CYP74 family
-
malfunction
-
loss-of-function mutant hpl3-1 produces disease-resembling lesions spreading through the whole leaves. Mutant hpl3-1 plants exhibit enhanced induction of jasmonic acid, trypsin proteinase inhibitors and other volatiles, but decreased levels of green leaf volatiles including (Z)-3-hexen-1-ol. Mutant hpl3-1 plants are more attractive to a BPH egg parasitoid, Anagrus nilaparvatae, than the wild-type, most likely as a result of increased release of BPH-induced volatiles. Mutant hpl3-1 plants also show increased resistance to bacterial blight (Xanthomonas oryzae pv. oryzae)
malfunction
silencing HPL in wild-type Solanum lycopersicum increases potato aphid (Macrosiphum euphorbiae) host preference and reproduction on 5-week-old plants but has no influence on 3-week-old plants. Silencing HPL in spr2 mutants does not compromise this aphid resistance. Moreover, a mutation in the FAD7 gene in Arabidopsis thaliana also confers resistance to the green peach aphid (Myzus persicae) in a genetic background that carries a null mutation in HPL
malfunction
the mutant enzyme preferentially utilises 9-hydroperoxylinoleic acid
malfunction
the mutant enzyme preferentially utilises 9-hydroperoxylinoleic acid. Multiple mutations of the hydroperoxide-binding domain leading to the TCFNSF motif virtually do not alter the specificity of catalysis compared to the wild-type enzyme. Conversely, the L97F variant offers good allene oxide synthase (AOS) activity with 9-hydroperoxylinoleic acid (9-HPOD)
metabolism
AOS is involved in jasmonic acid biosynthesis. AOS1 operates acid biosynthesis predominantly
metabolism
-
role for Phe137 in catalysis, mutation to Leu switches the product outcome from AOS to hydroperoxide lyase
metabolism
AOS is involved in the jasmonate biochemical pathway, detailed overview
metabolism
-
the enzymes are involved in the biosynthesis of (8R,11S)-dihydroxylinoleic acid via isomerization of (8R)-hydroperoxylinoleic acid to (5S,8R)-dihydroxylinoleic acid and to (8R,11S)-dihydroxylinoleic acid by abstraction of the pro-S hydrogens at C-5 and C-11 of (8R)-hydroperoxylinoleic acid, respectively, followed by suprafacial oxygenation
metabolism
-
allene oxide synthase and its relationship to the catalytic cycle of cytochrome P450s, overview
metabolism
-
allene oxide synthase is an intermediary enzyme in the octadecanoid pathway involved in conversion of (13S,9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid to allene oxid
metabolism
allene oxide synthase is involved in jasmonic acid biosynthesis
metabolism
-
jasmonic acid is synthesized from linolenic acid (18:3n-3) by sequential action of 13-lipoxygenase, allene oxide synthase, and allene oxide cyclase
metabolism
allene oxide synthase (AOS) and 13-hydroperoxide lyase (HPL) pathways, are best recognized as producers of defense compounds against biotic challenges, role of these two oxylipin branches in plant tolerance to the abiotic stress, namely excessive light, overview. Allen oxide synthase (AOS) and hydroperoxide lyase (HPL), the two enzymes functional in parallel branches of oxylipin pathway, compete for the common substrate hydroperoxide of linolenic acid (i.e. (9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid)
metabolism
-
allene oxide synthase (AOS) and 13-hydroperoxide lyase (HPL) pathways, are best recognized as producers of defense compounds against biotic challenges, role of these two oxylipin branches in plant tolerance to the abiotic stress, namely excessive light, overview. Allen oxide synthase (AOS) and hydroperoxide lyase (HPL), the two enzymes functional in parallel branches of oxylipin pathway, compete for the common substrate hydroperoxide of linolenic acid (i.e. 13-hydroperoxy-(9Z,11E,15Z)-octadecatrienoic acid)
metabolism
enzyme HPL is important in the biochemical pathway for synthesis of C6 volatiles in Solanum lycopersicum, pathway overview
metabolism
enzyme HPL1 competes with allene oxide synthase (AOS) for lipid-bound hydroperoxide fatty acids. The last step in the synthesis of galactolipid-bound OPDA and dnOPDA from unstable allene oxides is exclusively enzyme-catalyzed and not the result of spontaneous cyclization. All steps in arabidopside biosynthesis are enzyme-dependent and apparently all reactions can take place with substrates being esterified to galactolipids
metabolism
HPL-mediated GLV metabolism in tea plant, overview
metabolism
hydroperoxide lyase (HPL) is an enzyme found in higher plants that is involved in a lipid oxidation pathway, called the lipoxygenase pathway, which is activated in response to wounds or pathogen attacks
metabolism
the enzyme is involved in the lipoxygenase (LOX) pathway
metabolism
-
jasmonic acid is synthesized from linolenic acid (18:3n-3) by sequential action of 13-lipoxygenase, allene oxide synthase, and allene oxide cyclase
-
metabolism
-
allene oxide synthase (AOS) and 13-hydroperoxide lyase (HPL) pathways, are best recognized as producers of defense compounds against biotic challenges, role of these two oxylipin branches in plant tolerance to the abiotic stress, namely excessive light, overview. Allen oxide synthase (AOS) and hydroperoxide lyase (HPL), the two enzymes functional in parallel branches of oxylipin pathway, compete for the common substrate hydroperoxide of linolenic acid (i.e. (9Z,11E,15Z)-13-hydroperoxy-9,11,15-octadecatrienoic acid)
-
metabolism
-
jasmonic acid is synthesized from linolenic acid (18:3n-3) by sequential action of 13-lipoxygenase, allene oxide synthase, and allene oxide cyclase
-
metabolism
-
jasmonic acid is synthesized from linolenic acid (18:3n-3) by sequential action of 13-lipoxygenase, allene oxide synthase, and allene oxide cyclase
-
physiological function
expressed AOS2 protein is not obtained in soluble form
physiological function
-
is a cytochrome P450
physiological function
-
is a potential rubber transferase, the enzyme polymerizes thousands of isoprenes into molecules of rubber. Plays no role in jasmonate biosynthesis
physiological function
-
plays a role in jasmonate biosynthesis
physiological function
-
plays a role in jasmonate biosynthesis
physiological function
-
plays a role in jasmonate biosynthesis
physiological function
the lipoxygenase-catalyzed addition of molecular oxygen to alpha-linolenic acid initiates jasmonate synthesis by providing a 13-hydroperoxide substrate for formation of an unstable allene oxide by allene oxide synthase. This allene oxide then undergoes enzyme-guided cyclization to produce 12-oxophytodienoic acid. Phe137 stabilizes the carbon-centered radical intermediate, which is essential for AOS activity
physiological function
-
role for the rice enzyme in mediating plant-specific defense responses. OsHPL3 possesses intrinsic hydroperoxide lyase activity hydrolyzing hydroperoxylinolenic acid to produce green leaf volatiles, that play diverse roles in plant defense responses against insect pests and pathogens. OsHPL3 positively modulates resistance to the rice brown planthopper, Nilaparvata lugens, but negatively modulates resistance to the rice striped stem borer, Chilo suppressalis (Walker)
physiological function
-
the enzyme is involved in synthesis of green note substances from linoleic acid and alpha-linolenic acid in the plant
physiological function
-
the enzyme plays an important role in regulation of allene oxide synthase level and activity in pearl millet upon Sclerospora graminicola infection
physiological function
fatty acid hydroperoxide lyase (HPO lyase) is an enzyme widely found in plants and vegetables. HPO lyase is involved in the biosynthesis of volatile aldehydes and alcohols. It catalyses the breakdown of fatty acid hydroperoxides to generate omega-oxo-acids and aldehydes (C6 or C9 aldehydes) which are used industrially to reconstitute the fresh green odor of fruits and vegetables lost during processing
physiological function
green leaf volatiles (GLVs) are C6-aliphatic aldehydes/alcohols/acetates, and biosynthesized from the central precursor fatty acid 13-hydroperoxides by 13-hydroperoxide lyases (HPLs) in various plant species. While GLVs have been implicated as defense compounds in plants, GLVs give characteristic grassy note to a bouquet of aroma in green tea, which is manufactured from young leaves of Camellia sinensis. Gene CYP74B24 encodes tea HPL enzyme. Constitutive expression of CYP74B24 gene in intact tea leaves might account for low but substantial and constitutive formation of a subset of GLVs, some of which are stored as glycosides
physiological function
green leaf volatiles (GLVs) are the main contributors to the characteristic odor of plants known under the name of green note. GLVs are naturally produced through a metabolic pathway of the C18-polyunsaturated fatty acids named the lipoxygenase pathway. First, the lipoxygenase (LOX) catalyzes the oxygenation of linoleic and linolenic acids to form corresponding fatty acid hydroperoxides which are then cleaved by hydroperoxide lyase (HPL) to generate short-chain aldehydes and oxoacids. GLVs are widely used by various industries to improve food quality by restoring the fresh and fruity green odor or to add a touch of freshness to fragrances. The C6-aldehyde compounds are the main components (about 80 %) of the virgine olive oil flavor
physiological function
hydroperoxide lyase (HPL) is an enzyme found in higher plants that is involved in a lipid oxidation pathway, called the lipoxygenase pathway, which is activated in response to wounds or pathogen attacks. Volatile C6-aldehydes and C9-aldehydes produced by HPLs and their corresponding alcohols are known as green leaf volatiles (GLVs) and are responsible for the fresh green odor of many fruits and vegetables. GLVs such as hexanal, (Z)-3-hexenal, and (E)-2-hexenal are associated to the green note odor that is of major importance in the fragrance and flavor industries. They are also widely used in the food and beverage industry to restore the fresh green character lost during processing or to enhance food storage due to their antimicrobial activities
physiological function
-
hydroperoxide lyase (HPL) is the major enzyme in the biosynthesis of natural volatile aldehydes and alcohols in plants. The enzyme is important for defense against insects in tea plants
physiological function
-
role for the hydroperoxide lyase branch of the oxylipin biosynthesis pathway in protecting the photosynthetic apparatus under high light conditions potentially exerted through tight regulation of free linolenic acid and 13-hydroperoxy linolenic acid levels, as well as competition with production of metabolites by the allene oxide synthase (AOS)-branch of the oxylipin pathway
physiological function
role for the hydroperoxide lyase branch of the oxylipin biosynthesis pathway in protecting the photosynthetic apparatus under high light conditions potentially exerted through tight regulation of free linolenic acid and 13-hydroperoxy linolenic acid levels, as well as competition with production of metabolites by the allene oxide synthase (AOS)-branch of the oxylipin pathway
physiological function
the activity of hydroperoxide lyase 1 (HPL1) regulates the accumulation of galactolipids containing 12-oxo-phytodienoic acid in Arabidopsis thaliana. Galactolipids containing esters of 12-oxo-phytodienoic acid (OPDA) and dinor-12-oxo-phytodienoic acid (dnOPDA) are referred to as arabidopsides (chloroplast membrane lipids containing (dn)OPDA) and accumulate in response to abiotic and biotic stress. Expression analysis of enzyme HPL1 shows large differences in transcript abundance between accessions C24 and Col-0. Accession C24 is identified as a poor accumulator of arabidopsides whereas the commonly used accession Col-0 is found to accumulate comparably large amounts of arabidopsides in response to tissue damage
physiological function
the HPL pathway can influence direct defenses against insects, volatiles (E)-2-hexenal, hexanol, (E)-2-hexenol, and (Z)-3-hexenol reduce aphid fecundity. HPL contributes to certain forms of aphid resistance in tomato, but that the effects of fatty acid desaturase 7 (FAD7) on aphids in tomato and Arabidopsis are distinct from and independent of HPL. Disrupted function of FAD7, confers resistance to the potato aphid (Macrosiphum euphorbiae) and modifies the plant's C6 volatile profiles in Solanum lycopersicum. Moreover, a mutation in the FAD7 gene in Arabidopsis thaliana also confers resistance to the green peach aphid (Myzus persicae) in a genetic background that carries a null mutation in HPL
physiological function
-
role for the hydroperoxide lyase branch of the oxylipin biosynthesis pathway in protecting the photosynthetic apparatus under high light conditions potentially exerted through tight regulation of free linolenic acid and 13-hydroperoxy linolenic acid levels, as well as competition with production of metabolites by the allene oxide synthase (AOS)-branch of the oxylipin pathway
-
additional information
-
putative type II ligand-induced spin state transition in OsAOS1
additional information
the acid-alcohol pair Glu946-Ser949 lacks catalytic importance for the allene oxide synthase activity
additional information
-
the acid-alcohol pair Glu946-Ser949 lacks catalytic importance for the allene oxide synthase activity
additional information
the enzyme has the distal heme signature sequence of Thr-His
additional information
-
the enzyme has the distal heme signature sequence of Thr-His
additional information
exogenously applied oxylipins (free linolenic acid (LA) and linolenic acid hydroperoxide (13-HPOT), AOS branch metabolites: 12-OPDA and methyl derivative of jasmonic acid (Me-JA), and HPL-branch metabolites: trans-2-hexenal, cis-3-hexenol, cis-3-hexenyl acetate, and traumatic acid (TA)) alter photochemical activity of intact leaves of growing Arabidopsis plants, overview. Cis-3-hexenal is excluded from the analysis
additional information
-
exogenously applied oxylipins (free linolenic acid (LA) and linolenic acid hydroperoxide (13-HPOT), AOS branch metabolites: 12-OPDA and methyl derivative of jasmonic acid (Me-JA), and HPL-branch metabolites: trans-2-hexenal, cis-3-hexenol, cis-3-hexenyl acetate, and traumatic acid (TA)) alter photochemical activity of intact leaves of growing Arabidopsis plants, overview. Cis-3-hexenal is excluded from the analysis
additional information
-
exogenously applied oxylipins (free linolenic acid (LA) and linolenic acid hydroperoxide (13-HPOT), AOS branch metabolites: 12-OPDA and methyl derivative of jasmonic acid (Me-JA), and HPL-branch metabolites: trans-2-hexenal, cis-3-hexenol, cis-3-hexenyl acetate, and traumatic acid (TA)) alter photochemical activity of isolated thylakoid membranes, overview. Cis-3-hexenal is excluded from the analysis
additional information
three-dimensional modelling of CYP74s and structure comparisons
additional information
three-dimensional modelling of CYP74s and structure comparisons
additional information
three-dimensional modelling of CYP74s and structure comparisons
additional information
three-dimensional modelling of CYP74s and structure comparisons
additional information
three-dimensional modelling of CYP74s and structure comparisons
additional information
transformation of Col-0 plants with the C24 HPL1 allele under transcriptional regulation of the 35S promoter reveals a strong negative correlation between HPL1 expression and arabidopside accumulation after tissue damage. A quantitative trait loci analysis of an F2 population created from a cross between C24 and Col-0 locates a region on chromosome four strongly linked to the capacity to form arabidopsides
additional information
-
exogenously applied oxylipins (free linolenic acid (LA) and linolenic acid hydroperoxide (13-HPOT), AOS branch metabolites: 12-OPDA and methyl derivative of jasmonic acid (Me-JA), and HPL-branch metabolites: trans-2-hexenal, cis-3-hexenol, cis-3-hexenyl acetate, and traumatic acid (TA)) alter photochemical activity of intact leaves of growing Arabidopsis plants, overview. Cis-3-hexenal is excluded from the analysis
-
additional information
-
the enzyme has the distal heme signature sequence of Thr-His
-
additional information
-
the acid-alcohol pair Glu946-Ser949 lacks catalytic importance for the allene oxide synthase activity
-
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.
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.
Hamberg, M.
Biosynthesis of 12-oxo-10,15(Z)-phytodienoic acid: identification of an allene oxide cyclase
Biochem. Biophys. Res. Commun.
156
543-550
1988
Zea mays
brenda
Su, C.; Sahlin, M.; Oliw, E.H.
A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities
J. Biol. Chem.
273
20744-20751
1998
Gaeumannomyces graminis
brenda
Brodowsky, I.D.; Hamberg, M.; Oliw, E.H.
BW A4C and other hydroxamic acids are potent inhibitors of linoleic acid 8R-dioxygenase of the fungus Gaeumannomyces graminis
Eur. J. Pharmacol.
254
43-47
1994
Gaeumannomyces graminis
brenda
Su, C.; Brodowsky, I.D.; Oliw, E.H.
Studies on linoleic acid 8R-dioxygenase and hydroperoxide isomerase of the fungus Gaeumannomyces graminis
Lipids
30
43-50
1995
Gaeumannomyces graminis
brenda
Hamberg, M.; Zhang, L.Y.; Brodowsky, I.D.; Oliw, E.H.
Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: Stereochemistry of dioxygenase and hydroperoxide isomerase reactions
Arch. Biochem. Biophys.
309
77-80
1994
Gaeumannomyces graminis
brenda
Hamberg, M.
Mechanism of corn hydroperoxide isomerase: detection of 12,13(S)-oxido-9(Z),11-octadecanoic acid
Biochim. Biophys. Acta
920
76-84
1987
Zea mays
-
brenda
Kermasha, S.; Van de Voort, F.R.; Metche, M.
Conversion of linoleic acid hydroperoxide by French bean hydroperoxide isomerase
J. Food Biochem.
10
285-303
1986
Phaseolus vulgaris
-
brenda
Feng, P.; Vick, B.A.; Zimmerman, D.C.
Formation of gamma-ketols from 13- and 9-hydroxyperoxides of linoleic acid by flaxseed hydroperoxide isomerase
Lipids
16
377-379
1981
Linum usitatissimum
-
brenda
Gardner, H.W.
Stereospecificity of linoleic acid hydroperoxide isomerase from corn germ
Lipids
14
208-211
1979
Zea mays
-
brenda
Lulai, E.C.; Baker, C.W.; Zimmerman, D.C.
Metabolism of linoleic acid by barley lipoxygenase and hydroperoxide isomerase
Plant Physiol.
68
950-955
1981
Hordeum vulgare
brenda
Hamberg, M.; Gerwick, W.H.
Biosynthesis of vicinal dihydroxy fatty acids in the red alga Gracilariopsis menaneiformis: Identification of a sodium-dependent 12-lipoxygenase and a hydroperxide isomerase
Arch. Biochem. Biophys.
305
115-122
1993
Gracilariopsis lemaneiformis
brenda
Hamberg, M.
Fatty acid hydroperoxide isomerase in Saprolegnia parasitica: Structural studies of epoxy alcohols formed from isomeric hydroperoxyoctadecadienoates
Lipids
24
249-255
1989
Saprolegnia parasitica
-
brenda
Grossman, S.; Bergman, M.; Sofer, Y.
Purification and partial characterization of eggplant linoleate hydroperoxide isomerase
Biochim. Biophys. Acta
752
65-72
1983
Solanum melongena, Zea mays
-
brenda
Yabuuchi, S.; Amaha, M.
Partial purification and characterization of the linoleate hydroperoxide isomerase from grains of Hordeum distichum
Phytochemistry
15
387-390
1976
Hordeum vulgare subsp. vulgare
-
brenda
Heimann, W.; Dresen, P.
Uber den enzymatischen Hydroperoxidabbau in Cerealien Enzymcharakterisierung and Reaktionsprodukte
Helv. Chim. Acta
56
463-469
1973
Avena sativa
-
brenda
Reynaud, D.; Ali, M.; Demin, P.; Pace-Asciak, C.R.
Formation of 14,15-hepoxilins of the A(3) and B(3) series through a 15-lipoxygenase and hydroperoxide isomerase present in garlic roots
J. Biol. Chem.
274
28213-28218
1999
Allium sativum
brenda
Yu, Z.; Schneider, C.; Boeglin, W.E.; Marnett, L.J.; Brash, A.R.
The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase
Proc. Natl. Acad. Sci. USA
100
9162-9167
2003
Homo sapiens
brenda
Kupfer, R.; Liu, S.Y.; Allentoff, A.J.; Thompson, J.A.
Comparisons of hydroperoxide isomerase and monooxygenase activities of cytochrome P450 for conversions of allylic hydroperoxides and alcohols to epoxyalcohols and diols: probing substrate reorientation in the active site
Biochemistry
40
11490-11501
2001
Rattus norvegicus
brenda
Hamberg, M.
Hydroperoxide isomerases
J. Lipid Mediat. Cell Signal.
12
283-292
1995
Gaeumannomyces graminis, Gracilariopsis lemaneiformis, Saprolegnia parasitica
brenda
Cristea, M.; Oliw, E.H.
A G316A mutation of manganese lipoxygenase augments hydroperoxide isomerase activity: mechanism of biosynthesis of epoxyalcohols
J. Biol. Chem.
281
17612-17623
2006
Gaeumannomyces graminis (Q8X151)
brenda
Chawengsub, Y.; Aggarwal, N.T.; Nithipatikom, K.; Gauthier, K.M.; Anjaiah, S.; Hammock, B.D.; Falck, J.R.; Campbell, W.B.
Identification of 15-hydroxy-11,12-epoxyeicosatrienoic acid as a vasoactive 15-lipoxygenase metabolite in rabbit aorta
Am. J. Physiol. Heart Circ. Physiol.
294
H1348-H1356
2008
Oryctolagus cuniculus
brenda
Jiang, K.; Pi, Y.; Hou, R.; Zeng, H.; Huang, Z.; Zhang, Z.; Sun, X.; Tang, K.
Molecular cloning and expression profiling of the first specific jasmonate biosynthetic pathway gene allene oxide synthase from Lonicera japonica
Mol. Biol. Rep.
36
487-493
2009
Lonicera japonica (A1X873), Lonicera japonica
brenda
Lee, D.; Nioche, P.; Hamberg, M.; Raman, C.S.
Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes
Nature
455
363-368
2008
Arabidopsis thaliana (Q96242), Arabidopsis thaliana
brenda
Siqueira-Junior, C.L.; Jardim, B.C.; Urmenyi, T.P.; Vicente, A.C.; Hansen, E.; Otsuki, K.; da Cunha, M.; Madureira, H.C.; de Carvalho, D.R.; Jacinto, T.
Wound response in passion fruit (Passiflora f. edulis flavicarpa) plants: gene characterization of a novel chloroplast-targeted allene oxide synthase up-regulated by mechanical injury and methyl jasmonate
Plant Cell Rep.
27
387-397
2008
Passiflora edulis (A7XY79), Passiflora edulis
brenda
Bandara, P.K.; Takahashi, K.; Sato, M.; Matsuura, H.; Nabeta, K.
Cloning and functional analysis of an allene oxide synthase in Physcomitrella patens
Biosci. Biotechnol. Biochem.
73
2356-2359
2009
Physcomitrium patens (A9S014), Physcomitrium patens (A9SNA2), Physcomitrium patens
brenda
Brash, A.
Mechanistic aspects of CYP74 allene oxide synthases and related cytochrome P450 enzymes
Phytochemistry
70
1522-1531
2009
Arabidopsis thaliana, Linum usitatissimum, Solanum lycopersicum, Parthenium argentatum, Solanum tuberosum, Zea mays, Acaryochloris marina
brenda
Cho, K.B.; Lai, W.; Hamberg, M.; Raman, C.S.; Shaik, S.
The reaction mechanism of allene oxide synthase: interplay of theoretical QM/MM calculations and experimental investigations
Arch. Biochem. Biophys.
507
14-25
2011
Arabidopsis thaliana
brenda
Jernern, F.; Garscha, U.; Hoffmann, I.; Hamberg, M.; Oliw, E.H.
Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
Aspergillus clavatus
brenda
Mukhtarova, L.S.; Mukhitova, F.K.; Gogolev, Y.V.; Grechkin, A.N.
Hydroperoxide lyase cascade in pea seedlings: Non-volatile oxylipins and their age and stress dependent alterations
Phytochemistry
72
356-364
2011
Pisum sativum
brenda
Gfeller, A.; Dubugnon, L.; Liechti, R.; Farmer, E.
Jasmonate biochemical pathway
Sci. Signal.
109
1-6
2010
Arabidopsis thaliana (Q96242), Arabidopsis thaliana
brenda
Jerneren, F.; Eng, F.; Hamberg, M.; Oliw, E.H.
Linolenate 9R-dioxygenase and allene oxide synthase activities of Lasiodiplodia theobromae
Lipids
47
65-73
2012
Lasiodiplodia theobromae, Lasiodiplodia theobromae 2334
brenda
Buchhaupt, M.; Guder, J.C.; Etschmann, M.M.; Schrader, J.
Synthesis of green note aroma compounds by biotransformation of fatty acids using yeast cells coexpressing lipoxygenase and hydroperoxide lyase
Appl. Microbiol. Biotechnol.
93
159-168
2012
Citrullus lanatus
brenda
Yoeun, S.; Rakwal, R.; Han, O.
Dual positional substrate specificity of rice allene oxide synthase-1: insight into mechanism of inhibition by type II ligand imidazole
BMB Rep.
46
151-156
2013
Oryza sativa
brenda
Toporkova, Y.Y.; Ermilova, V.S.; Gorina, S.S.; Mukhtarova, L.S.; Osipova, E.V.; Gogolev, Y.V.; Grechkin, A.N.
Structure-function relationship in the CYP74 family: conversion of divinyl ether synthases into allene oxide synthases by site-directed mutagenesis
FEBS Lett.
587
2552-2558
2013
Linum usitatissimum, Nicotiana tabacum
brenda
Boeglin, W.E.; Brash, A.R.
Cytochrome P450-type hydroxylation and epoxidation in a tyrosine-liganded hemoprotein, catalase-related allene oxide synthase
J. Biol. Chem.
287
24139-24147
2012
Plexaura homomalla
brenda
Hoffmann, I.; Jerneren, F.; Oliw, E.H.
Expression of fusion proteins of Aspergillus terreus reveals a novel allene oxide synthase
J. Biol. Chem.
288
11459-11469
2013
Aspergillus terreus (Q0CW98), Aspergillus terreus, Aspergillus terreus A1156 (Q0CW98)
brenda
Brash, A.R.; Niraula, N.P.; Boeglin, W.E.; Mashhadi, Z.
An ancient relative of cyclooxygenase in cyanobacteria is a linoleate 10S-dioxygenase that works in tandem with a catalase-related protein with specific 10S-hydroperoxide lyase activity
J. Biol. Chem.
289
13101-13111
2014
Nostoc punctiforme (B2J5P3)
brenda
Bruehlmann, F.; Bosijokovic, B.; Ullmann, C.; Auffray, P.; Fourage, L.; Wahler, D.
Directed evolution of a 13-hydroperoxide lyase (CYP74B) for improved process performance
J. Biotechnol.
163
339-345
2013
Psidium guajava
brenda
Hoffmann, I.; Oliw, E.H.
Discovery of a linoleate 9S-dioxygenase and an allene oxide synthase in a fusion protein of Fusarium oxysporum
J. Lipid Res.
54
3471-3480
2013
Fusarium oxysporum (F9F4K7), Fusarium oxysporum, Fusarium oxysporum Fo5176 (F9F4K7)
brenda
Hosur Gnanaprakash, P.; Jogaiah, S.; Sreedhara, A.P.; Nagraj Prashanth, G.; Kini, R.K.; Shetty, S.H.
Association between accumulation of allene oxide synthase activity and development of resistance against downy mildew disease of pearl millet
Mol. Biol. Rep.
40
6821-6829
2013
Cenchrus americanus
brenda
Padilla, M.N.; Hernandez, M.L.; Sanz, C.; Martinez-Rivas, J.M.
Stress-dependent regulation of 13-lipoxygenases and 13-hydroperoxide lyase in olive fruit mesocarp
Phytochemistry
102
80-88
2014
Olea europaea
brenda
Huang, F.C.; Schwab, W.
Overexpression of hydroperoxide lyase, peroxygenase and epoxide hydrolase in tobacco for the biotechnological production of flavours and polymer precursors
Plant Biotechnol. J.
10
1099-1109
2012
Cucumis melo
brenda
Tong, X.; Qi, J.; Zhu, X.; Mao, B.; Zeng, L.; Wang, B.; Li, Q.; Zhou, G.; Xu, X.; Lou, Y.; He, Z.
The rice hydroperoxide lyase OsHPL3 functions in defense responses by modulating the oxylipin pathway
Plant J.
71
763-775
2012
Oryza sativa
brenda
Knopf, R.R.; Feder, A.; Mayer, K.; Lin, A.; Rozenberg, M.; Schaller, A.; Adam, Z.
Rhomboid proteins in the chloroplast envelope affect the level of allene oxide synthase in Arabidopsis thaliana
Plant J.
72
559-571
2012
Arabidopsis thaliana (Q96242), Arabidopsis thaliana
brenda
Panagakou, I.; Touloupakis, E.; Ghanotakis, D.F.
Structural characterization of hydroperoxide lyase in dodecyl maltoside by using circular dichroism
Protein J.
32
1-6
2013
Capsicum annuum
brenda
Teder, T.; Boeglin, W.E.; Schneider, C.; Brash, A.R.
A fungal catalase reacts selectively with the 13S fatty acid hydroperoxide products of the adjacent lipoxygenase gene and exhibits 13S-hydroperoxide-dependent peroxidase activity
Biochim. Biophys. Acta
1862
706-715
2017
Fusarium graminearum (I1REW2), Fusarium graminearum, Fusarium graminearum PH-1 (I1REW2)
brenda
Jacopini, S.; Mariani, M.; de Caraffa, V.B.; Gambotti, C.; Vincenti, S.; Desjobert, J.M.; Muselli, A.; Costa, J.; Berti, L.; Maury, J.
Olive recombinant hydroperoxide lyase, an efficient biocatalyst for synthesis of green leaf volatiles
Appl. Biochem. Biotechnol.
179
671-683
2016
Olea europaea (G8XQN2)
brenda
Jacopini, S.; Vincenti, S.; Mariani, M.; Brunini-Bronzini de Caraffa, V.; Gambotti, C.; Desjobert, J.M.; Muselli, A.; Costa, J.; Tomi, F.; Berti, L.; Maury, J.
Activation and stabilization of olive recombinant 13-hydroperoxide lyase using selected additives
Appl. Biochem. Biotechnol.
182
1000-1013
2017
Olea europaea (G8XQN2)
brenda
Toporkova, Y.Y.; Gorina, S.S.; Bessolitsyna, E.K.; Smirnova, E.O.; Fatykhova, V.S.; Bruehlmann, F.; Ilyina, T.M.; Mukhtarova, L.S.; Grechkin, A.N.
Double function hydroperoxide lyases/epoxyalcohol synthases (CYP74C) of higher plants identification and conversion into allene oxide synthases by site-directed mutagenesis
Biochim. Biophys. Acta
1863
369-378
2018
Cucumis sativus (A0A0A0K2U8), Cucumis sativus (U5YTM6), Solanum tuberosum (C7ENW3), Glycine max (M4WFN0), Medicago truncatula (Q7X9B3), Cucumis melo (Q93XR3)
brenda
Liu, Q.; Hua, Y.
Continuous synthesis of hexanal by immobilized hydroperoxide lyase in packed-bed reactor
Bioprocess Biosyst. Eng.
38
2439-2449
2015
Amaranthus tricolor
brenda
Santiago-Gomez, P.M.; Vergely, C.; Policar, C.; Nicaud, J.-M.; Belin, J.-M.; Rochette, L.; Husson, F.
Characterization of purified green bell pepper hydroperoxide lyase expressed by Yarrowia lipolytica radicals detection during catalysis
Enzyme Microb. Technol.
41
13-18
2007
Capsicum annuum (Q39443)
-
brenda
Li, J.; Avila, C.A.; Tieman, D.M.; Klee, H.J.; Goggin, F.L.
A Comparison of the effects of fatty acid desaturase and hydroperoxide lyase on plant-aphid interactions
Int. J. Mol. Sci.
19
E1077
2018
Solanum lycopersicum (Q9XGI8)
brenda
Deng, W.W.; Wu, Y.L.; Li, Y.Y.; Tan, Z.; Wei, C.L.
Molecular Cloning and characterization of hydroperoxide lyase gene in the leaves of tea plant (Camellia sinensis)
J. Agric. Food Chem.
64
1770-1776
2016
Camellia sinensis
brenda
Gargouri, M.; Drouet, P.; Legoy, M.-D.
Hydroperoxide-lyase activity in mint leaves volatile C6-aldehyde production from hydroperoxy-fatty acids
J. Biotechnol.
111
59-65
2004
Mentha spicata, Mentha pulegium
brenda
Nilsson, A.K.; Fahlberg, P.; Johansson, O.N.; Hamberg, M.; Andersson, M.X.; Ellerstroem, M.
The activity of hydroperoxide lyase 1 regulates accumulation of galactolipids containing 12-oxo-phytodienoic acid in Arabidopsis
J. Exp. Bot.
67
5133-5144
2016
Arabidopsis thaliana (B3LF83)
brenda
Ono, E.; Handa, T.; Koeduka, T.; Toyonaga, H.; Tawfik, M.M.; Shiraishi, A.; Murata, J.; Matsui, K.
CYP74B24 is the 13-hydroperoxide lyase involved in biosynthesis of green leaf volatiles in tea (Camellia sinensis)
Plant Physiol. Biochem.
98
112-118
2016
Camellia sinensis (G4VV60), Camellia sinensis
brenda
Savchenko, T.; Yanykin, D.; Khorobrykh, A.; Terentyev, V.; Klimov, V.; Dehesh, K.
The hydroperoxide lyase branch of the oxylipin pathway protects against photoinhibition of photosynthesis
Planta
245
1179-1192
2017
Spinacia oleracea, Arabidopsis thaliana (B3LF83), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (B3LF83)
brenda