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(8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
conversion of (8R)-hydroperoxylinoleic acid into (7S,8S)-dihydroxylinoleic acid by stereospecific elimination of the pro-S hydrogen from C-7 and intramolecular suprafacial insertion of oxygen at C-7
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate

(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate

(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-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
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-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
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase (the recombinant enzyme forms 5,8(R)-dihydroxylinoleic acid (60% 5S) and 8(R),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
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase (the recombinant enzyme forms 5,8(R)-dihydroxylinoleic acid (60% 5S) and 8(R),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
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
(8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate

(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-10,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate

(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
Q9UUS2
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
Q9UUS2
-
-
-
?
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
(7S,8S,9Z,12Z)-7,8-dihydroxy-9,12-octadecadienoate
-
-
-
-
?
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glycoprotein

-
7,8-LDS contains five tentative N-linked glycosylation sites, one of which has high probability of glycosylation. This N-glycosylation site, Asn216, is located near the distal heme-binding region along with tentative sites for O-linked glycosylation. Asn216Gln shows no detectable enzyme activity, although expression of Asn216Gln is confirmed by Western blot analysis. alpha-Mannosidase treatment does not change the 8R-dioxygenase activity but abolishes the hydroperoxide isomerase activity. Proper N- and O-linked glycosylation could be important for the hydroperoxide isomerase. Expression of 7,8-LDS in insect cells yields recombinant 7,8-LDS with the native hydroperoxide isomerase activity; 7,8-LDS contains five tentative N-linked glycosylation sites, one of which has high probability of glycosylation. This N-glycosylation site, Asn216, is located near the distal heme-binding region along with tentative sites for O-linked glycosylation. Asn216Gln shows no detectable enzyme activity, although expression of Asn216Gln is confirmed by Western blot analysis. alpha-Mannosidase treatment does not change the 8R-dioxygenase activity but abolishes the hydroperoxide isomerase activity. Proper N- and O-linked glycosylation could be important for the hydroperoxide isomerase. Expression of 7,8-LDS in insect cells yields recombinant 7,8-LDS with the native hydroperoxide isomerase activity
glycoprotein
-
7,8-LDS contains five tentative N-linked glycosylation sites, one of which has high probability of glycosylation. This N-glycosylation site, Asn216, is located near the distal heme-binding region along with tentative sites for O-linked glycosylation. Asn216Gln shows no detectable enzyme activity, although expression of Asn216Gln is confirmed by Western blot analysis. alpha-Mannosidase treatment does not change the 8R-dioxygenase activity but abolishes the hydroperoxide isomerase activity. Proper N- and O-linked glycosylation could be important for the hydroperoxide isomerase. Expression of 7,8-LDS in insect cells yields recombinant 7,8-LDS with the native hydroperoxide isomerase activity; 7,8-LDS contains five tentative N-linked glycosylation sites, one of which has high probability of glycosylation. This N-glycosylation site, Asn216, is located near the distal heme-binding region along with tentative sites for O-linked glycosylation. Asn216Gln shows no detectable enzyme activity, although expression of Asn216Gln is confirmed by Western blot analysis. alpha-Mannosidase treatment does not change the 8R-dioxygenase activity but abolishes the hydroperoxide isomerase activity. Proper N- and O-linked glycosylation could be important for the hydroperoxide isomerase. Expression of 7,8-LDS in insect cells yields recombinant 7,8-LDS with the native hydroperoxide isomerase activity
-
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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)
brenda
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
14738-14745
1992
Gaeumannomyces graminis
brenda
Hörnsten, 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)
brenda
Brodowsky, I.D.; Hamberg, M.; Oliw, E.H.
BW A4C and other hydroxamic acids are potent inhibitors of linoleic acid 8R-dioxygenase of the fungus Gaeumannomyces graminis
Eur. J. Pharmacol.
254
43-47
1994
Gaeumannomyces graminis
brenda
Su, C.; Brodowsky, I.D.; Oliw, E.H.
Studies on linoleic acid 8R-dioxygenase and hydroperoxide isomerase of the fungus Gaeumannomyces graminis
Lipids
30
43-50
1995
Gaeumannomyces graminis
brenda
Hamberg, M.; Zhang, L.Y.; Brodowsky, I.D.; Oliw, E.H.
Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: Stereochemistry of dioxygenase and hydroperoxide isomerase reactions
Arch. Biochem. Biophys.
309
77-80
1994
Gaeumannomyces graminis, Gaeumannomyces graminis var.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 (Q9UUS2), Gaeumannomyces graminis var. avenae, Gaeumannomyces graminis var. avenae (Q9UUS2)
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