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Information on EC 1.13.11.60 - linoleate 8R-lipoxygenase
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1.13.11.60 linoleate 8R-lipoxygenaseIUBMB Comments
The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P-450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) . The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) .
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Word Map
- 1.13.11.60
- hydroperoxide
- graminis
-
gaeumannomyces
- oxylipins
-
dioxygenation
-
antarafacial
-
8r-hydroperoxylinoleic
-
allene
-
aspergilli
-
suprafacial
-
cyclooxygenases
-
ppoas
- verticillioides
-
take-all
-
homolytic
-
zymoseptoria
-
ferryl
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
linoleate diol synthase, 7,8-lds, 5,8-lds, 8r-dioxygenase, 8r-dox, 7,8-linoleate diol synthase, dioxygenase-cytochrome p450, 8(r)-dioxygenase, 8r-dox-5,8-lds, 5,8-linoleate diol synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5,8-LDS
5,8-linoleate diol synthase
6,8-diol synthase
6R,8R-linoleate diol synthase
6R,8RLDS
7,8-diol synthase
7,8-LDS
7,8-linoleate diol synthase
8(R)-dioxygenase
8,11-hydroperoxide isomerase
8-DOX
8R-dioxygenase
8R-DOX
8R-DOX-5,8-LDS
8R-DOX-LDS
dioxygenase-cytochrome P450
DOX-CYP
EC 1.13.11.44
-
-
formerly, part transferred
-
FOXB_09952
GLRG_10013
linoleate diol synthase
orphan DOX-CYP
PpoA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
linoleate:oxygen (8R)-oxidoreductase
The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P-450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) [1]. The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(11Z)-icos-11-enoic acid + O2
10-hydroperoxyeicosenoic acid
-
-
-
?
(11Z,14Z)-icosa-11,14-dienoic acid + O2
(11Z,14Z)-10-hydroperoxyeicosa-11,14-dienoic acid
-
-
-
?
(11Z,14Z,17Z)-icosa-11,14,17-trienoic acid + O2
(11Z,14Z,17Z)-10-hydroperoxyeicosa-11,14,17-trienoic acid
-
-
-
?
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoate + O2
(8R,11R)-8,11-dihydroperoxy-(9Z,12Z)-octadecadienoate + (7R,8R)-7,8-dihydroperoxy-(9Z,12Z)-octadecadienoate
alpha-linolenate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12,15-octadecatrienoate
-
-
-
?
alpha-linolenate + O2
(9Z,12Z,15Z)-7,8-dihydroperoxyoctadeca-9,12,15-trienoate
via (9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoate, whole enzyme reaction
-
-
?
alpha-linolenate + O2
(9Z,12Z,15Z)-7,8-dihydroxyoctadeca-9,12,15-trienoic acid
via (9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoic acid, best substrate with respect to whole enzyme activity
-
-
?
alpha-linolenate + O2
(9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoate
dioxygenase reaction of the N-terminal domain
-
-
?
alpha-linolenic acid + O2
(6Z,8E,12Z)-10-hydroperoxyoctadecatrienoic acid
-
-
-
?
alpha-linolenic acid + O2
8(9)epoxy-10-hydroxy-(12Z,15Z)-octadecadienoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,14Z)-8-hydroxyeicosa-5,8,11,14-tetraenoic acid
-
-
-
?
arachidonic acid + O2
8-hydroxyarachidonic acid
-
-
-
?
dihomo-gamma-linolenate + O2
(8Z,11Z,14Z)-8-hydroxyeicosa-8,11,14-trienoic acid
-
-
-
?
dihomo-gamma-linolenic acid + O2
8-hydroxydihomo-gamma-linolenic acid
-
-
-
?
eicosadienoate + O2
(11Z,14Z)-8-hydroxyeicosa-11,14-dienoic acid
-
-
-
?
eicosadienoic acid + O2
8-hydroxyeicosadienoic acid
-
-
-
?
eicosenoate + O2
(11Z)-8-hydroxyeicosa-11-enoic acid
-
-
-
?
eicosenoic acid + O2
8-hydroxyeicosenoic acid
-
-
-
?
linoleate + O2
(8E,12Z)-10-hydroperoxyoctadeca-8,12-dienoic acid + (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoate + (8R,11R)-8,11-dihydroperoxy-(9Z,12Z)-octadecadienoate + (7R,8R)-7,8-dihydroperoxy-(9Z,12Z)-octadecadienoate
-
-
-
?
oleate + O2
(9Z)-8-hydroperoxyoctadeca-9-enoic acid
dioxygenase reaction of the N-terminal domain
-
-
?
oleate + O2
8-hydroperoxyoctadecamonoenoate + 7,8-dihydroxyoctadecamonoenoate
-
-
-
?
palmitoleate + O2
(9Z)-5,8-dihydroxyhexadeca-9-enoic acid
via (9Z)-dihydroperoxyhexadeca-9-enoate
-
-
?
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoate + O2
(8R,11R)-8,11-dihydroperoxy-(9Z,12Z)-octadecadienoate + (7R,8R)-7,8-dihydroperoxy-(9Z,12Z)-octadecadienoate
-
-
-
?
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoate + O2
(8R,11R)-8,11-dihydroperoxy-(9Z,12Z)-octadecadienoate + (7R,8R)-7,8-dihydroperoxy-(9Z,12Z)-octadecadienoate
-
-
-
?
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoate + O2
(8R,11R)-8,11-dihydroperoxy-(9Z,12Z)-octadecadienoate + (7R,8R)-7,8-dihydroperoxy-(9Z,12Z)-octadecadienoate
Colletotrichum graminicola M1.001 / M2 / FGSC 10212
-
-
-
?
alpha-linolenic acid + O2
(6S,8R,9Z,12Z,15Z)-dihydroxy-9,12,15-octadecatrienoic acid
-
-
-
-
?
alpha-linolenic acid + O2
(6S,8R,9Z,12Z,15Z)-dihydroxy-9,12,15-octadecatrienoic acid
Penicillium oxalicum KCTC 6440
-
-
-
-
?
arachidonic acid + O2
(R)-10-hydroxyarachidonic acid
-
-
-
?
docosapentaenoic acid + O2
(R)-10-hydroperoxy-docosapentaenoic acid
-
-
-
?
docosapentaenoic acid + O2
(R)-10-hydroperoxy-docosapentaenoic acid
-
-
-
?
gamma-linolenic acid + O2
(R)-8-hydroxy-gamma-linolenic acid
-
-
-
?
gamma-linolenic acid + O2
(R)-8-hydroxy-gamma-linolenic acid
-
-
-
?
linoleate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
via (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, whole enzyme reaction, best substrate
-
-
r
linoleate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
Colletotrichum gloeosporioides KACC 40961
via (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, whole enzyme reaction, best substrate
-
-
r
linoleate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
r
linoleate + O2
(7S,8S)-7,8-dihydroxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
linoleate + O2
(7S,8S)-7,8-dihydroxy-(9Z,12Z)-octadecadienoic acid
-
-
-
-
?
linoleate + O2
(7S,8S)-7,8-dihydroxy-(9Z,12Z)-octadecadienoic acid
Colletotrichum gloeosporioides KACC 40961
-
-
-
?
linoleate + O2
(8R)-hydroxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
linoleate + O2
(8R)-hydroxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
linoleate + O2
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate. Mechanism of biosynthesis: the enzyme oxidizes linoleic acid to (8R)-hydroperoxylinoleic acid and to (5S,8R)-dihydroxylinoleic acids as major products. This occurs by abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-8 or at C-10 with double bond migration. (8R,9Z,12Z)-8-Hydroperoxy-9,12-octadecadienoate is then isomerized to (5S,8R,9Z,12Z)-5,8-dihydroperoxy-9,12-octadecadienoate by abstraction of the pro-S hydrogen at C-5 of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate, respectively, followed by suprafacial oxygenation
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
the enzyme is involved in the regulation of the life cycle of Aspergillus nidulans. Synthesis of the psi factor (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate, that influences the development of the asexual conidiophores and sexual cleistothecia
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The N-terminal heme peroxidase domain might be responsible for the dioxygenase reaction as the first step of the PpoA reaction, i.e. oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate as an intermediate product. The C-terminal P450 domain catalyzes the second reaction step, the isomerization of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (5S,8R,9Z,12Z)-5,8-dihydroperoxy-9,12-octadecadienoate, and is therefore termed the 8-hydroperoxide isomerase P450 domain
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
Colletotrichum gloeosporioides KACC 40961
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate
the wild-type enzyme forms 98% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate and 2% (10R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate. The V330L mutation augments the formation of (10R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate 3fold
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
bifunctional enzyme with linoleic acid (8R)-dioxygenase and hydroperoxide isomerase activities. The enzyme abstracts the 8-pro-S hydrogen from linoleic acid, which is followed by antarafacial insertion of molecular oxygen at C-8 to generate 8R-hydroperoxylinoleate. The latter is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate by elimination of the 7-pro-S hydrogen and intramolecular suprafacial insertion of an oxygen atom from the hydroperoxide group
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
bifunctional enzyme with linoleic acid 8R-dioxygenase and hydroperoxide isomerase activities. The enzyme abstracts the 8-pro-S hydrogen from linoleic acid, which is followed by antarafacial insertion of molecular oxygen at C-8 to generate 8R-hydroperoxylinoleate. The latter is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate by elimination of the 7-pro-S hydrogen and intramolecular suprafacial insertion of an oxygen atom from the hydroperoxide group
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase. The recombinant enzyme forms (5S,8R)-dihydroxylinoleic acid (60% 5S) and 8R,13-dihydroxyoctadeca-(9E,11E)-dienoic acid possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8R-dioxygenase activity is identical with native 7,8-linoleate diol synthase
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
H2O2 (up to 9 mM) does not support enzyme activity under anaerobic conditions
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The dioxygenase reaction involves stereospecific abstraction of the pro-S hydrogen from C-8 followed by antarafacial insertion of dioxygen to produce (8R)-hydroperoxylinoleic acid
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase. The recombinant enzyme forms (5S,8R)-dihydroxylinoleic acid (60% 5S) and 8R,13-dihydroxyoctadeca-(9E,11E)-dienoic acid possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8R-dioxygenase activity is identical with native 7,8-linoleate diol synthase
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
bifunctional enzyme with linoleic acid (8R)-dioxygenase and hydroperoxide isomerase activities. The enzyme abstracts the 8-pro-S hydrogen from linoleic acid, which is followed by antarafacial insertion of molecular oxygen at C-8 to generate 8R-hydroperoxylinoleate. The latter is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate by elimination of the 7-pro-S hydrogen and intramolecular suprafacial insertion of an oxygen atom from the hydroperoxide group
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
bifunctional enzyme with linoleic acid 8R-dioxygenase and hydroperoxide isomerase activities. The enzyme abstracts the 8-pro-S hydrogen from linoleic acid, which is followed by antarafacial insertion of molecular oxygen at C-8 to generate 8R-hydroperoxylinoleate. The latter is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate by elimination of the 7-pro-S hydrogen and intramolecular suprafacial insertion of an oxygen atom from the hydroperoxide group
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate. The dioxygenase reaction involves stereospecific abstraction of the pro-S hydrogen from C-8 followed by antarafacial insertion of dioxygen to produce (8R)-hydroperoxylinoleic acid
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
all-cis-9,12-octadecadienoic acid
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
dioxygenase reaction of the N-terminal domain
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Colletotrichum gloeosporioides KACC 40961
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Colletotrichum gloeosporioides KACC 40961
dioxygenase reaction of the N-terminal domain
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
the enzyme oxidizes linoleate and the Gly conjugate rapidly to hydroperoxides at C-8 but also at C-9 and C-13 (ratio 1:0.1:0.2, respectively) and to 7,8-diol
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Penicillium oxalicum KCTC 6440
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid
-
-
-
?
linoleic acid + O2
(6R,8R)-dihydroxy-9,12(Z,Z)-octadecadienoic acid
-
highest activity
-
-
?
linoleic acid + O2
(6R,8R)-dihydroxy-9,12(Z,Z)-octadecadienoic acid
Penicillium oxalicum KCTC 6440
-
highest activity
-
-
?
oleate + O2
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
via (9Z)-8-hydroperoxyoctadeca-9-enoic acid
-
-
?
oleate + O2
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
via (9Z)-8-hydroperoxyoctadeca-9-enoic acid, whole enzyme reaction
-
-
?
oleate + O2
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
-
-
-
?
oleate + O2
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
palmitoleate + O2
(9Z)-8-hydroperoxyhexadec-9-enoate
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-
-
?
palmitoleate + O2
(9Z)-8-hydroperoxyhexadec-9-enoate
Colletotrichum gloeosporioides KACC 40961
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-
-
?
palmitoleic acid + O2
(6S,8R,9Z)-dihydroxy-9-hexadecenoic acid
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-
-
-
?
palmitoleic acid + O2
(6S,8R,9Z)-dihydroxy-9-hexadecenoic acid
Penicillium oxalicum KCTC 6440
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-
-
-
?
additional information
?
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-
the bifunctional enzyme forms 5S,8S-dihydroxylinoleic acid from (8R)-hydroperoxylinoleic acid by intramolecular oxygen transfer. Linoleate diol synthases are fungal dioxygenase-cytochrome P450 fusion enzymes. P450 hydroxylases usually contain an acid-alcohol pair in the I-helices for the heterolytic scission of O2 and formation of compound I, i.e. Por+-Fe(IV)=O, and water. The function of the acid-alcohol pair appears to be replaced by a different amide residue, Gln890 of 5,8-LDS, for heterolysis of (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate to generate compound I
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-
?
additional information
?
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-
the enzyme forms (5S,8R)-5,8-dihydroxylinoleic acid from (8R)-hydroperoxylinoleic acid by intramolecular oxygen transfer. Linoleate diol synthases are fungal dioxygenase-cytochrome P450 fusion enzymes
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-
?
additional information
?
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bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
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-
?
additional information
?
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-
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
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-
?
additional information
?
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the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, and oleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5S,8R,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase
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?
additional information
?
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-
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, and oleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5S,8R,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase
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-
?
additional information
?
-
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
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-
?
additional information
?
-
-
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
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-
?
additional information
?
-
Colletotrichum gloeosporioides KACC 40961
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
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-
?
additional information
?
-
Colletotrichum gloeosporioides KACC 40961
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
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-
?
additional information
?
-
Colletotrichum gloeosporioides KACC 40961
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, and oleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5S,8R,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase
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?
additional information
?
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enzyme oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases, but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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?
additional information
?
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enzyme oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases, but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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?
additional information
?
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no substrate: gamma-linolenoate
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?
additional information
?
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-
no substrate: gamma-linolenoate
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?
additional information
?
-
the dioxygenase-cytochrome P450 homologue oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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-
?
additional information
?
-
-
the dioxygenase-cytochrome P450 homologue oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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-
?
additional information
?
-
enzyme oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases, but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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-
?
additional information
?
-
no substrate: gamma-linolenoate
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-
?
additional information
?
-
the dioxygenase-cytochrome P450 homologue oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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-
?
additional information
?
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Colletotrichum graminicola M1.001 / M2 / FGSC 10212
enzyme oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases, but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
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-
?
additional information
?
-
Colletotrichum graminicola M1.001 / M2 / FGSC 10212
no substrate: gamma-linolenoate
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-
?
additional information
?
-
Colletotrichum graminicola M1.001 / M2 / FGSC 10212
the dioxygenase-cytochrome P450 homologue oxidizes oleic and linoleic acids in analogy with 7,8-linoleate diol synthases (LDSs), but with the additional biosynthesis of 8,11-dihydroxylinoleic acid
-
-
?
additional information
?
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enzyme metabolizes fatty acids to hydroperoxides with broad substrate specificity. Products show R configuration at the (n-10) positions. Fatty acids of the n-3 series are oxidized less efficiently and often to hydroperoxides with an R configuration at both (n-10) and (n-7) positions
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-
?
additional information
?
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-
enzyme metabolizes fatty acids to hydroperoxides with broad substrate specificity. Products show R configuration at the (n-10) positions. Fatty acids of the n-3 series are oxidized less efficiently and often to hydroperoxides with an R configuration at both (n-10) and (n-7) positions
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-
?
additional information
?
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enzyme metabolizes fatty acids to hydroperoxides with broad substrate specificity. Products show R configuration at the (n-10) positions. Fatty acids of the n-3 series are oxidized less efficiently and often to hydroperoxides with an R configuration at both (n-10) and (n-7) positions
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?
additional information
?
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the recombinant enzyme expressed in insect cells, oxygenates 16:1n-7, 18:1n-7, 18:2n-6, 18:3n-3, 20:1n-9, 20:1n-11, and 20:2n-6 at the allylic carbon closest to the carboxyl group
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-
?
additional information
?
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the bifunctional enzyme forms (7S,8S)-7,8-dihydroxylinoleic acid from (8R)-hydroperoxylinoleic acid by intramolecular oxygen transfer. Linoleate diol synthases are fungal dioxygenase-cytochrome P450 fusion enzymes. P450 hydroxylases usually contain an acid-alcohol pair in the I-helices for the heterolytic scission of O2 and formation of compound I, i.e. Por+-Fe(IV)=O, and water. The function of the acid-alcohol pair appears to be replaced by a different amide residue, Asn938 of 7,8-LDS, for heterolysis of (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate to generate compound I
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-
?
additional information
?
-
the Ile and Trp conjugates of linoleate are not oxidized at C-8. The enzyme oxidizes the linoleate-Ile conjugate to 9- and 13-HODE-Ile and to 9(10)- and 12(13)epoxyalcohols. The alpha-linolenic acid-Ile conjugate is transformed to 9-, 13-, and 16-HOTrE-Ile in a ratio of 0.4:0.3:1, respectively
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
linoleate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
r
linoleate + O2
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
oleate + O2
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
i.e. (9Z,12Z)-octadeca-9,12-dienoate
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
the enzyme is involved in the regulation of the life cycle of Aspergillus nidulans. Synthesis of the psi factor (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate, that influences the development of the asexual conidiophores and sexual cleistothecia
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-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate