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(11Z)-icos-11-enoic acid + O2
10-hydroperoxyeicosenoic acid
-
-
-
?
(11Z)-icosa-11-enoate + O2
?
-
-
-
?
(11Z,14Z)-icosa-11,14-dienoic acid + O2
(11Z,14Z)-10-hydroperoxyeicosa-11,14-dienoic acid
-
-
-
?
(11Z,14Z)-icosa-11,14-dienoic acid + O2
?
-
-
-
?
(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-linolenate + O2
?
-
-
-
?
alpha-linolenic acid + O2
(6S,8R,9Z,12Z,15Z)-dihydroxy-9,12,15-octadecatrienoic acid
alpha-linolenic acid + O2
(6Z,8E,12Z)-10-hydroperoxyoctadecatrienoic acid
-
-
-
?
alpha-linolenic acid + O2
8(9)epoxy-10-hydroxy-(12Z,15Z)-octadecadienoate
-
-
-
?
alpha-linolenic acid + O2
?
arachidonate + O2
(5Z,8Z,11Z,14Z)-8-hydroxyeicosa-5,8,11,14-tetraenoic acid
-
-
-
?
arachidonic acid + O2
(R)-10-hydroxyarachidonic 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
-
-
-
?
docosapentaenoic acid + O2
(R)-10-hydroperoxy-docosapentaenoic 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
-
-
-
?
gamma-linolenic acid + O2
(R)-8-hydroxy-gamma-linolenic acid
linoleate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
linoleate + O2
(7S,8S)-7,8-dihydroxy-(9Z,12Z)-octadecadienoic acid
linoleate + O2
(8E,12Z)-10-hydroperoxyoctadeca-8,12-dienoic acid + (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(8R)-hydroxy-(9Z,12Z)-octadecadienoic acid
linoleate + O2
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid
linoleate + O2
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoate + (8R,11R)-8,11-dihydroperoxy-(9Z,12Z)-octadecadienoate + (7R,8R)-7,8-dihydroperoxy-(9Z,12Z)-octadecadienoate
-
-
-
?
linoleic acid + O2
(6R,8R)-dihydroxy-9,12(Z,Z)-octadecadienoic acid
oleate + O2
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
oleate + O2
(9Z)-8-hydroperoxyoctadec-9-enoate
oleate + O2
(9Z)-8-hydroperoxyoctadeca-9-enoic acid
dioxygenase reaction of the N-terminal domain
-
-
?
oleate + O2
8-hydroperoxyoctadecamonoenoate + 7,8-dihydroxyoctadecamonoenoate
-
-
-
?
oleic acid + O2
(6R,8R,9Z)-dihydroxy-9-octadecenoic acid
palmitoleate + O2
(9Z)-5,8-dihydroxyhexadeca-9-enoic acid
via (9Z)-dihydroperoxyhexadeca-9-enoate
-
-
?
palmitoleate + O2
(9Z)-8-hydroperoxyhexadec-9-enoate
palmitoleate + O2
?
-
-
-
?
palmitoleic acid + O2
(6S,8R,9Z)-dihydroxy-9-hexadecenoic acid
additional information
?
-
(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
-
-
-
?
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
-
-
-
-
?
alpha-linolenic acid + O2
?
-
-
-
?
alpha-linolenic acid + O2
?
-
-
-
?
alpha-linolenic acid + O2
?
-
-
-
?
arachidonic acid + O2
(R)-10-hydroxyarachidonic acid
-
-
-
?
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
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
?
oleate + O2
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
oleate + O2
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
oleic acid + O2
(6R,8R,9Z)-dihydroxy-9-octadecenoic acid
-
-
-
-
?
oleic acid + O2
(6R,8R,9Z)-dihydroxy-9-octadecenoic acid
-
-
-
-
?
palmitoleate + O2
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleate + O2
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleate + O2
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleic acid + O2
(6S,8R,9Z)-dihydroxy-9-hexadecenoic acid
-
-
-
-
?
palmitoleic acid + O2
(6S,8R,9Z)-dihydroxy-9-hexadecenoic acid
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
?
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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, 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
?
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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, 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
?
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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, 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
?
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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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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
?
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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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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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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
?
-
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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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
?
-
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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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
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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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C1006S
the hydroperoxide isomerase activity of 5,8-LDS mutant is abolished
C1006S/V328F
the mutant forms after reduction of hydroperoxides to alcohols, (8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid and (10R)-hydroxy-(8E,12Z)-octadecadienoic acid in the same relative amounts
C1006S/V328L
the mutant forms after reduction of hydroperoxides to alcohols, (8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid and (10R)-hydroxy-(8E,12Z)-octadecadienoic acid in the same relative amounts
C1006S/V328S
the mutant forms after reduction of hydroperoxides to alcohols, (8R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid and (10R)-hydroxy-(8E,12Z)-octadecadienoic acid in the same relative amounts
N887L
-
site-directed mutagenesis, the mutant retains (5S,8R)-5,8-dihydroxylinoleate as the main metabolite with an increased formation of 6,8- and 8,11-dihydroxylinoleate
N887Q
-
site-directed mutagenesis, the mutant retains (5S,8R)-5,8-dihydroxylinoleate as the main metabolite with an increased formation of 6,8- and 8,11-dihydroxylinoleate
Q890E
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site-directed mutagenesis, the mutant retains (5S,8R)-5,8-dihydroxylinoleate as the main product, but shifts oxygenation from C-5 to C-7 and C-11 and to formation of epoxyalcohols by homolytic scission of (8R)-hydroperoxylinoleic acid
Q890L
-
site-directed mutagenesis, the mutant shows almost abolished 5,8-linoleate diol synthase activity
Y374F
mutation in the conserved sequence YRWH results in loss of linoleate 8R-lipoxygenase activity, whereas the hydroperoxide isomerase activity is retained
H1004A
mutant enzyme with abolished 8-hydroperoxide isomerase activity, whereas dioxygenase activity is still present
Y374
the mutant enzyme shows no detectable activity when incubated with (9Z,12Z)-octadeca-9,12-dienoate as a substrate. When incubated with the intermediate product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate it is able to catalyze isomerization to (5S,8R,9Z,12Z)-5,8-dihydroperoxy-9,12-octadecadienoate
A891G
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
C1038S
site-directed mutagenesis, the mutant produces a low amount of 7,8-DiHODE with the accumulation of 8-HPODE
H1036A
site-directed mutagenesis, the mutant produces a low amount of 7,8-DiHODE with the accumulation of 8-HPODE
H1036A/C1038S
site-directed mutagenesis, the double mutant converts linoleic acid to only 8-HPODE
N895D
site-directed mutagenesis, the mutant produces a reduced amount of 8-HPODE, compared to wild-type, without the accumulation of DiHODE
N895L
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
N895Q
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Q898E
site-directed mutagenesis, the mutant converts linoleic acid to 8,11-DiHODE as major product and 7,8-DiHODE as minor product
Q898L
site-directed mutagenesis, the mutant converts linoleic acid to 8,11-DiHODE as major product and 7,8-DiHODE as minor product
Y380F
site-directed mutagenesis, the mutant enzyme produces trace amount of 7,8-DiHODE without the accumulation of 8-HPODE when incubated with linoleic acid as substrate
A891G
-
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
-
N895D
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site-directed mutagenesis, the mutant produces a reduced amount of 8-HPODE, compared to wild-type, without the accumulation of DiHODE
-
N895L
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site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
-
Y380F
-
site-directed mutagenesis, the mutant enzyme produces trace amount of 7,8-DiHODE without the accumulation of 8-HPODE when incubated with linoleic acid as substrate
-
E384A
-
mutant forms only traces of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
I375A
-
mutant has virtually no dioxygenase activity
K540L
inactive mutant enzyme
K540Q
inactive mutant enzyme
K540R
inactive mutant enzyme
L334V
-
inactive mutant enzyme
N216Q
-
inactive mutant enzyme, no 8(R)-dioxygenase activity
N938D
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site-directed mutagenesis, the mutation of the 7,8-linoleate diol synthase reduces the hydroperoxide isomerase activity of the enzyme
N938L
-
site-directed mutagenesis, the mutation of the 7,8-linoleate diol synthase abolishes the hydroperoxide isomerase activity of the enzyme
N938Q
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site-directed mutagenesis, the mutation of the 7,8-linoleate diol synthase reduces the hydroperoxide isomerase activity of the enzyme
V330L
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the wild-type enzyme forms 98% (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate and 2% (8E,10R,12Z)-10-hydroperoxy-9,12-octadecadienoate. The V330L mutation augments the formation of (8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate 3fold
Y329L
inactive mutant enzyme
Y376F
inactive mutant enzyme
Y378F
inactive mutant enzyme
Y378S
inactive mutant enzyme
Y531F
inactive mutant enzyme
H379Q
-
inactive mutant enzyme, no 8(R)-dioxygenase activity
-
N216Q
-
inactive mutant enzyme, no 8(R)-dioxygenase activity
-
C1005S
-
the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
D749A
-
the mutant shows less than 10% activity of the wild type enzyme
E728A
-
the mutant shows less than 10% activity of the wild type enzyme
F794E
-
the mutant acts as 7,8-linoleate diol synthase
F794Y
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the mutant shows less than 10% activity of the wild type enzyme
F798Y
-
the mutant shows less than 10% activity of the wild type enzyme
H1003A
-
the mutant shows less than 10% activity of the wild type enzyme
I841A
-
the mutant shows more than 110% activity of the wild type enzyme
L970A
-
the mutant shows more than 110% activity of the wild type enzyme
M1051A
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the mutant shows more than 110% activity of the wild type enzyme
M695A
-
the mutant shows more than 110% activity of the wild type enzyme
M883A
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the mutant shows more than 110% activity of the wild type enzyme
N886D
-
the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
P1016A
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the mutant shows more than 110% activity of the wild type enzyme
Q887A
-
the mutant shows less than 10% activity of the wild type enzyme
R707A
-
the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
R814A
-
the mutant shows less than 10% activity of the wild type enzyme
R934A
-
the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
T879A
-
the mutant shows more than 110% activity of the wild type enzyme
V1010A
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the mutant shows more than 110% activity of the wild type enzyme
V884A
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the mutant shows more than 110% activity of the wild type enzyme
Y690F
-
the mutant shows less than 10% activity of the wild type enzyme
F794E
-
the mutant acts as 7,8-linoleate diol synthase
-
I841A
-
the mutant shows more than 110% activity of the wild type enzyme
-
M695A
-
the mutant shows more than 110% activity of the wild type enzyme
-
H379Q
inactive mutant enzyme
H379Q
-
inactive mutant enzyme, no 8(R)-dioxygenase activity
Q889A
-
the mutant acts as 8,11-linoleate diol synthase
Q889A
-
the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
Q889A
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the mutant acts as 8,11-linoleate diol synthase
-
Q889A
-
the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
-
additional information
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replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolishes 8R-dioxygenase (8-DOX) and hydroperoxide isomerase activities, respectively. Val328 of 5,8-LDS does not influence the position of oxygenation
additional information
replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolishes 8R-dioxygenase (8-DOX) and hydroperoxide isomerase activities, respectively. Val328 of 5,8-LDS does not influence the position of oxygenation
additional information
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replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively. N-terminal expression constructs of 5,8- and 7,8-LDS (674 of 1079, and 673 of 1165 residues), containing one additional alpha-helix compared to cyclooxygenase-1, yields prominent 8R-DOX activities with apparently unchanged or slightly lower substrate affinities, respectively
additional information
replacements of Tyr and Cys in the conserved YRWH and FXXGPHXCLG sequences abolished 8R-dioxygenase and hydroperoxide isomerase activities, respectively. N-terminal expression constructs of 5,8- and 7,8-LDS (674 of 1079, and 673 of 1165 residues), containing one additional alpha-helix compared to cyclooxygenase-1, yields prominent 8R-DOX activities with apparently unchanged or slightly lower substrate affinities, respectively
additional information
comparison of substrate specificities of wild-type an d mutant enzymes, overview
additional information
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comparison of substrate specificities of wild-type an d mutant enzymes, overview
additional information
reaction conditions for the production of (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid from linoleic acid by recombinant Escherichia coli expressing 7,8-linoleate diol synthase from Glomerella cingulata are optimized using response surface methodology. The optimal reaction conditions are pH 7.0, 18.6°C, 10.8% v/v dimethyl sulfoxide, 44.9 g/l cells, and 14.3 g/l linoleic acid, with agitation at 256 rpm. Under these conditions, recombinant cells produce 7,8-dihydroxy-unsaturated fatty acids in the range of 7.0-9.8 g/l from 14.3 g/l linoleic acid, 14.3 g/l oleic acid, and plant oil hydrolysates such as waste oil and olive oil containing 14.3 g/l linoleic acid or oleic acid. Comparisons of quantitative production of dihydroxy unsaturated fatty acids by microorganisms
additional information
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reaction conditions for the production of (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid from linoleic acid by recombinant Escherichia coli expressing 7,8-linoleate diol synthase from Glomerella cingulata are optimized using response surface methodology. The optimal reaction conditions are pH 7.0, 18.6°C, 10.8% v/v dimethyl sulfoxide, 44.9 g/l cells, and 14.3 g/l linoleic acid, with agitation at 256 rpm. Under these conditions, recombinant cells produce 7,8-dihydroxy-unsaturated fatty acids in the range of 7.0-9.8 g/l from 14.3 g/l linoleic acid, 14.3 g/l oleic acid, and plant oil hydrolysates such as waste oil and olive oil containing 14.3 g/l linoleic acid or oleic acid. Comparisons of quantitative production of dihydroxy unsaturated fatty acids by microorganisms
additional information
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comparison of substrate specificities of wild-type an d mutant enzymes, overview
-
additional information
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reaction conditions for the production of (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid from linoleic acid by recombinant Escherichia coli expressing 7,8-linoleate diol synthase from Glomerella cingulata are optimized using response surface methodology. The optimal reaction conditions are pH 7.0, 18.6°C, 10.8% v/v dimethyl sulfoxide, 44.9 g/l cells, and 14.3 g/l linoleic acid, with agitation at 256 rpm. Under these conditions, recombinant cells produce 7,8-dihydroxy-unsaturated fatty acids in the range of 7.0-9.8 g/l from 14.3 g/l linoleic acid, 14.3 g/l oleic acid, and plant oil hydrolysates such as waste oil and olive oil containing 14.3 g/l linoleic acid or oleic acid. Comparisons of quantitative production of dihydroxy unsaturated fatty acids by microorganisms
-
additional information
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treatment with alpha-mannosidase to shorten N- and O-linked mannosides inhibis the hydroperoxide isomerase but not the 8(R)-dioxygenase
additional information
-
treatment with alpha-mannosidase to shorten N- and O-linked mannosides inhibis the hydroperoxide isomerase but not the 8(R)-dioxygenase
-
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Su, C.; Oliw, E.H.
Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as anovel hemoprotein
J. Biol. Chem.
271
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1996
Gaeumannomyces graminis (Q9UUS2)
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, Gaeumannomyces graminis (Q9UUS2), Gaeumannomyces graminis var. graminis, Gaeumannomyces graminis var. graminis (Q9UUS2)
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Brodowsky, I.D.; Hamberg, M.; Oliw, E.H.
A linoleic acid (8R)-dioxygenase and hydroperoxide isomerase of the fungus Gaeumannomyces graminis. Biosynthesis of (8R)-Hydroxylinoleic acid and (7S,8S)-dihydroxylinoleic acid from (8R)-Hydroperoxylinoleic acid
J. Biol. Chem.
267
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1992
Gaeumannomyces graminis
brenda
Hrnsten, L.; Su, C.; Osbourn, A.E.; Garosi, P.; Hellman, U.; Wernstedt, C.; Oliw, E.H.
Cloning of linoleate diol synthase reveals homology with prostaglandin H synthase
J. Biol. Chem.
274
28219-28224
1999
Gaeumannomyces graminis (Q9UUS2), 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
Brodowsky, I.D.; Zhang, L.Y.; Oliw, E.H.; Hamberg, M.
Linoleic acid 8R-dioxygenase and hydroperoxide isomerase of the fungus Gaeumannomyces graminis. Mechanism of catalysis and inhibition
Ann. N. Y. Acad. Sci.
744
314-316
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
Oliw, E.H.; Su, C.; Sahlin, M.
Catalytic properties of linoleate diol synthase of the fungus Gaeumannomyces graminis: A comparison with PGH synthases
Adv. Exp. Med. Biol.
469
679-685
1999
Gaeumannomyces graminis
brenda
Garscha, U.; Oliw, E.
Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase
Biochem. Biophys. Res. Commun.
373
579-583
2008
Gaeumannomyces graminis, Gaeumannomyces graminis var. avenae
brenda
Garscha, U.; Oliw, E.H.
Critical amino acids for the 8(R)-dioxygenase activity of linoleate diol synthase. A comparison with cyclooxygenases
FEBS Lett.
582
3547-3551
2008
Gaeumannomyces graminis (Q9UUS2)
brenda
Brodhun, F.; Goebel, C.; Hornung, E.; Feussner, I.
Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450
J. Biol. Chem.
284
11792-11805
2009
Aspergillus nidulans (Q6RET3)
brenda
Garscha, U.; Oliw, E.H.
Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis oF (10R)-dioxygenase with epoxyalcohol synthase activity
J. Biol. Chem.
284
13755-13765
2009
Gaeumannomyces graminis
brenda
Hoffmann, I.; Jerneren, F.; Garscha, U.; Oliw, E.H.
Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase
Arch. Biochem. Biophys.
506
216-222
2010
Aspergillus fumigatus, Aspergillus fumigatus (C1KH66), Gaeumannomyces graminis
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
Hoffmann, I.; Oliw, E.H.
7,8- and 5,8-linoleate diol synthases support the heterolytic scission of oxygen-oxygen bonds by different amide residues
Arch. Biochem. Biophys.
539
87-91
2013
Aspergillus fumigatus, Gaeumannomyces graminis
brenda
Seo, M.J.; Shin, K.C.; An, J.U.; Kang, W.R.; Ko, Y.J.; Oh, D.K.
Characterization of a recombinant 7,8-linoleate diol synthase from Glomerella cingulate
Appl. Microbiol. Biotechnol.
100
3087-3099
2016
Colletotrichum gloeosporioides (A0A0S2SWE4), Colletotrichum gloeosporioides, Colletotrichum gloeosporioides KACC 40961 (A0A0S2SWE4)
brenda
Seo, M.J.; Kang, W.R.; Shin, K.C.; Oh, D.K.
Production of 7,8-dihydroxy unsaturated fatty acids from plant oils by whole recombinant cells expressing 7,8-linoleate diol synthase from Glomerella cingulata
J. Agric. Food Chem.
64
8555-8562
2016
Colletotrichum gloeosporioides (A0A0S2SWE4), Colletotrichum gloeosporioides, Colletotrichum gloeosporioides KACC 40961 (A0A0S2SWE4)
brenda
Sooman, L.; Oliw, E.H.
Discovery of a novel linoleate dioxygenase of Fusarium oxysporum and linoleate diol synthase of Colletotrichum graminicola
Lipids
50
1243-1252
2015
Colletotrichum graminicola (E3QVI1), Colletotrichum graminicola, Fusarium oxysporum (F9FU71), Fusarium oxysporum, Colletotrichum graminicola M1.001 (E3QVI1), Colletotrichum graminicola M1.001 / M2 / FGSC 10212 (E3QVI1), Fusarium oxysporum Fo5176 (F9FU71)
brenda
Oliw, E.H.
Linoleate diol synthase related enzymes of the human pathogens Histoplasma capsulatum and Blastomyces dermatitidis
Arch. Biochem. Biophys.
696
108669
2020
Paracoccidioides brasiliensis (A0A1E2Y953), Paracoccidioides brasiliensis, Blastomyces dermatitidis (F2TE78), Blastomyces dermatitidis
brenda
Oliw, E.H.
Polyunsaturated C18 fatty acids derivatized with Gly and Ile as an additional tool for studies of the catalytic evolution of fungal 8- and 9-dioxygenases
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1863
1378-1387
2018
Gaeumannomyces graminis (Q9UUS2)
brenda
Seo, M.J.; Kang, W.R.; Yang, E.J.; Shin, K.C.; Ko, Y.J.; Oh, D.K.
Molecular characterization of Penicillium oxalicum 6R,8R-linoleate diol synthase with new regiospecificity
Biochim. Biophys. Acta Mol. Cell Biol. Lipids
1864
577-586
2019
Penicillium oxalicum, Penicillium oxalicum KCTC 6440
brenda
Oliw, E.H.
Biosynthesis of oxylipins by Rhizoctonia solani with allene oxide and oleate 8S,9S-diol synthase activities
Lipids
53
527-537
2018
Rhizoctonia solani (A0A074S6K6), Rhizoctonia solani, Rhizoctonia solani 123E (A0A074S6K6)
brenda