1.13.11.60: linoleate 8R-lipoxygenase
This is an abbreviated version!
For detailed information about linoleate 8R-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.60
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1.13.11.60
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hydroperoxide
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graminis
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gaeumannomyces
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oxylipins
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dioxygenation
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antarafacial
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8r-hydroperoxylinoleic
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allene
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aspergilli
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suprafacial
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cyclooxygenases
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ppoas
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verticillioides
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take-all
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homolytic
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zymoseptoria
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ferryl
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synthesis
- 1.13.11.60
- hydroperoxide
- graminis
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gaeumannomyces
- oxylipins
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dioxygenation
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antarafacial
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8r-hydroperoxylinoleic
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allene
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aspergilli
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suprafacial
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cyclooxygenases
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ppoas
- verticillioides
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take-all
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homolytic
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zymoseptoria
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ferryl
- synthesis
Reaction
Synonyms
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-7,8-LDS, 8R-DOX-LDS, dioxygenase-cytochrome P450, DOX-CYP, EC 1.13.11.44, EGE82165, FOXB_09952, GLRG_10013, linoleate 7,8-LDS, linoleate 8,11-LDS, linoleate diol synthase, linoleic acid 8R-dioxygenase, ODH51007, orphan DOX-CYP, PpoA
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.11.60 - linoleate 8R-lipoxygenase
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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
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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
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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
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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
Colletotrichum gloeosporioides KACC 40961
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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
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N895D
Colletotrichum gloeosporioides KACC 40961
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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
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N895L
Colletotrichum gloeosporioides KACC 40961
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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
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Y380F
Colletotrichum gloeosporioides KACC 40961
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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
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E384A
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mutant forms only traces of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
H379Q
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
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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
C1005S
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the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
H1003A
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the mutant shows less than 10% activity of the wild type enzyme
I841A
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the mutant shows more than 110% activity of the wild type enzyme
L970A
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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
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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
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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
Q889A
R707A
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the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
R934A
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the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
T879A
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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
I841A
Penicillium oxalicum KCTC 6440
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the mutant shows more than 110% activity of the wild type enzyme
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M695A
Penicillium oxalicum KCTC 6440
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the mutant shows more than 110% activity of the wild type enzyme
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Q889A
additional information
Q889A
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the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
Q889A
Penicillium oxalicum KCTC 6440
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the variant exhibits only 8-HPODE formation without 6,8-DiHODE accumulation
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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
Colletotrichum gloeosporioides KACC 40961
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comparison of substrate specificities of wild-type an d mutant enzymes, overview
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additional information
Colletotrichum gloeosporioides KACC 40961
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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
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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
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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
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