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(10Z,13Z,16Z)-nonadeca-10,13,16-trienoic acid + O2
?
-
Substrates: oxidation at the n-6 carbon and at the bis-allylic position n-8
Products: -
?
(11Z,14Z)-eicosa-11,14-dienoic acid + O2
?
-
Substrates: LC-MS analysis shows that Fo-MnLOX oxidizes (11Z,14Z)-eicosa-11,14-dienoic acid efficiently at both C-15 and C-11
Products: -
?
(11Z,14Z)-eicosadienoic acid + O2
15-hydroxyperoxy-(9Z,11E)-eicosadienoic acid
-
Substrates: -
Products: -
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
15-hydroxyperoxy-11Z,13E,17Z-eicosatrienoic acid
-
Substrates: via 11-hydroperoxyoctadecadienoic acid, 13-hydroperoxyoctadecadienoic acid and 15-hydroperoxyoctadecadienoic acid
Products: -
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
?
(13R)-hydroperoxylinolenic acid + O2
13-ketolinolenic acid + epoxyalcohols
Substrates: only mutant enzyme G316A
Products: erythro- and threo-11-hydroxy-(12R,13R)-epoxy-(9Z,15Z)-octadecadienoic acids and one of the corresponding cis-epoxides as major products
?
(5E,8E,11E,14E)-icosa-5,8,11,14-tetraenoic acid + O2
(5Z,8Z,11S,12E,14Z)-11-hydroperoxyicosa-5,8,12,14-tetraenoic acid + (5Z,8Z,11Z,13E,15R)-15-hydroperoxyicosa-5,8,11,13-tetraenoic acid
-
Substrates: oxidation at the n-6 carbon and at the bis-allylic position n-8
Products: -
?
(5Z,8Z,11Z,14Z,17Z)-docosa-5,8,11,14,17-pentaenoate + O2
?
-
Substrates: oxidation at the n-6 carbon and at the bis-allylic position n-8
Products: -
?
(7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoate + O2
?
-
Substrates: oxidation at the n-6 carbon and at the bis-allylic position n-8
Products: -
?
(9E,12Z)-octadeca-9,12-dienoic acid + O2
?
-
Substrates: sLOX-1 oxidizes (9E,12Z)18:2 to 9-hydroperoxyoctadecadienoic acid in an R/S ratio of 60/40 and to 13-hydroperoxyoctadecadienoic acid
Products: -
?
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate + O2
(9Z,11E, 13R)-13-hydroperoxyoctadeca-9,11-dienoate
-
Substrates: -
Products: -
?
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate + O2
(9Z,11E,13R)-13-hydroperoxyoctadeca-9,11-dienoate
-
Substrates: -
Products: -
?
(9Z,12E)-octadeca-9,12-dienoic acid + O2
?
-
Substrates: sLOX-1 oxidizes (9Z,12E)18:2 slowly to the 9-hydroperoxy metabolite with 10E,12E configuration as the main product (65%) and to 13-hydroperoxyoctadecadienoic acid
Products: -
?
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
(9S)-hydroperoxy-octadeca-10,12-dienoate
-
Substrates: alpha-linoleate is converted via two intermediates, (11S)-hydroperoxy-(9Z,12Z)-octadecenoate and (13R)-hydroperoxy-(9Z,11E)-octadecadienoate, which are isomerized to the end product, probably after oxidation to peroxyl radicals, beta-fragmentation, and oxygen insertion at C-9
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(10E,12E,14E)-9,16-dihydroxy-octadeca-10,12,14-trienoate
-
Substrates: gamma-linoleate is oxidized at C-9, C-11, and C-13
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(13R)-hydroperoxyoctadecadienoic acid
-
Substrates: via bis-allylic 11S-hydroperoxy fatty acid
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
1,2-dilinoleoyl-phosphatidylcholine + O2
?
Substrates: a poor substrate
Products: -
?
1,2-dilinoleoyl-sn-glycero-3-phosphocholine + O2
?
-
Substrates: -
Products: main products with 14% and 10%, no production of 11-hydroxyoctadecanoic acid
?
1-linoleoyl-2-hydroxy-phosphatidylcholine + O2
?
Substrates: an excellent substrate
Products: -
?
1-linoleoyl-2-lyso-phosphatidylcholine + O2
?
-
Substrates: -
Products: -
?
1-linoleyl-lyso-glycerophosphatidylcholine + O2
11-hydroxyoctadecanoic acid + 13-hydroxyoctadecanoic acid
-
Substrates: via formation of the 13-hydroxyperoxy metabolite
Products: -
?
11-(11R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
9-(9R)-hydroperoxy-octadecadienoic acid
-
Substrates: slow
Products: -
?
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid methyl ester
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid methyl ester
-
Substrates: -
Products: -
?
11-hydroperoxyoctadecadienoic acid + O2
11,18-dihydroxy-12E,14Z,16E-eicosatrienoic acid
-
Substrates: -
Products: two diastereoisomers
?
alpha-linolenic acid + O2
(13R)-hydroperoxy octadecadienoic acid + 9-hydroperoxyoctadecadienoic acid
-
Substrates: -
Products: -
?
alpha-linolenic acid + O2
(9Z,11E,15Z)-(13)-hydroperoxyoctadecatrienoic acid
-
Substrates: -
Products: -
?
alpha-linolenic acid + O2
?
-
Substrates: -
Products: -
?
gamma-linolenic acid + O2
(6Z,9Z,11E)-(13)-hydroperoxyoctadecatrienoic acid + (6Z,9Z,12Z)-(11)-hydroperoxyoctadecatrienoic acid
-
Substrates: -
Products: -
?
linoleate + O2
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate
-
Substrates: -
Products: -
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid + (9Z,12Z)-(11S)-hydroperoxyoctadecadienoic acid
-
Substrates: -
Products: -
ir
linoleic acid + O2
?
-
Substrates: -
Products: -
?
linolenate + O2
(11R)-hydroperoxyoctadecadienoic acid + 13S-hydroperoxyoctadecadienoic acid + 9(S/R)-hydroperoxyoctadecadienoic acid
-
Substrates: Fo-MnLOX, with support of Ser348, binds linoleic acid so that the pro R rather than the pro S hydrogen at C-11 interacts with the metal center, but retains the suprafacial oxygenation mechanism observed in other MnLOXs
Products: -
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linolenate + O2
(11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
-
Substrates: -
Products: -
?
linolenic acid + O2
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
-
Substrates: -
Products: -
?
lyso-phosphatidylcholine + O2
?
additional information
?
-
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
?
-
Substrates: -
Products: -
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
?
-
Substrates: oxidation at the n-6 carbon and at the bis-allylic position n-8
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
-
Substrates: -
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
-
Substrates: oxidation at the bis-allylic n-5 carbon and at positions n-3, n-7, and n-6
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
-
Substrates: oxidation at the n-3 position
Products: -
?
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid
-
Substrates: 47% the rate of conversion of linolenic acid
Products: -
?
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid
-
Substrates: rapid
Products: -
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
Substrates: -
Products: -
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
Substrates: via bis-allylic 11S-hydroperoxy fatty acid
Products: -
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
Substrates: -
Products: -
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
Substrates: -
Products: -
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
Substrates: analysis of substrate conformation and environment, overview
Products: -
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
-
Substrates: -
Products: -
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
Substrates: -
Products: -
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
-
Substrates: -
Products: -
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
-
Substrates: -
Products: -
?
lyso-phosphatidylcholine + O2
?
-
Substrates: substrate from soybean
Products: -
?
lyso-phosphatidylcholine + O2
?
-
Substrates: substrate from soybean
Products: -
?
lyso-phosphatidylcholine + O2
?
Substrates: substrate from soybean
Products: -
?
additional information
?
-
-
Substrates: the 11-hydroperoxide does not undergo the rapid beta-fragmentation observed with 13R-MnLOX. Oxidation of [11S-2H]-linoleic acid by Cg-MnLOX is accompanied by loss of deuterium and a large kinetic isotope effect. Substrate specificity, overview
Products: -
?
additional information
?
-
-
Substrates: the 11-hydroperoxide does not undergo the rapid beta-fragmentation observed with 13R-MnLOX. No significant oxidation of (7Z,10Z,13Z)-hexadeca-7,10,13-trienoic acid, (6Z,9Z,12Z)-octadeca-6,9,12-trienoic acid, and arachidonic acid. The alpha-linolenic acid, which forms 11R-hydro(pero)xy-9Z,12Z,15Z-octadecatrienoic acid as a main metabolite, is oxidized to 9- and 13R-hydro(pero)xy-9Z,11E,15Z-octadecatrienoic acid at a much lower rate compared with linoleic acid, (11Z,14Z)-eicosa-11,14-dienoic acid, and (11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid. Substrate specificity, overview
Products: -
?
additional information
?
-
-
Substrates: Mn-LO likely binds fatty acids tail-first and oxygenates many C16, C18, C20, and C22 fatty acids to significant amounts of bis-allylic hydroperoxides. Unsaturated C16-C22 fatty acids, other than 18:3n-3, 18:2n-6, or 17:3n-3, are poor substrates, possibly because of ineffective enzyme activation through Mn2+ to Mn3+ by the produced hydroperoxides, substrate specificities of wild-type and mutant enzymes, overview
Products: -
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additional information
?
-
-
Substrates: the enzyme catalyzes the rearrangement of bis-allylic S-hydroxyperoxides to allylic R-hydroperoxides, and the oxygenation of 18:2n-6 by suprafacial hydrogen abstraction at C11 and O2 insertion at the bis-allylic position C11 and, with double bond migation, at the allylic position C13, overview, 20:4n-6 is a poor substrate, substrate specificities of wild-type and mutant enzymes, overview
Products: -
?
additional information
?
-
-
Substrates: 13R-MnLOX forms (11S)-hydroperoxyoctadecadienoic acid and (11R)-hydroperoxyoctadecatrienoic acid as intermediates during the linear phase of oxidation and the (13R)-hydroperoxides as main end products
Products: -
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additional information
?
-
-
Substrates: cf. EC 1.13.11.58, LC- and GC-MS analysis product analysis, overview
Products: -
?
additional information
?
-
-
Substrates: oxidation of 18:1 n-6 is performed by 13R-MnLOX
Products: -
?
additional information
?
-
-
Substrates: (9Z,12E)18:2 is not oxidized at a detectable rate. sLOX-1 oxidizes (9E,12Z)18:2 more efficiently than (9Z,12E)18:2
Products: -
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additional information
?
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Substrates: the enzyme can also convert linoleate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate, cf. linoleate 9S-lipoxygenase/EC 1.13.11.58 and linoleate 13R-lipoxygenase. Oxygen consumption monitoring
Products: -
?
additional information
?
-
-
Substrates: the enzyme can also convert linoleate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate, cf. linoleate 9S-lipoxygenase/EC 1.13.11.58 and linoleate 13R-lipoxygenase. Oxygen consumption monitoring
Products: -
?
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L530R
-
site-directed mutagenesis
S348F
-
site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme
F337I
-
site-directed mutagenesis, replacement of Phe337 with Ile changes the stereochemistry of the 13-hydroperoxy metabolites of 18:2n-6 and 18:3n-3 (from 100% R to 69-74% S) with little effect on regiospecificity. The abstraction of the pro-S hydrogen of 18:2n-6 is retained, suggesting antarafacial hydrogen abstraction and oxygenation. The mutant shows highly reduced activity compared to the wild-type enzyme
F347A
-
site-directed mutagenesis, the mutant oxidizes octadeca-9,11-dienoic acid to 11-hydroperoxyoctadecadienoate/(13R)-hydroperoxyoctadecadienoate/(9S)-hydroperoxyoctadecadienoate in an initial ratio of 50/42/8 and with almost complete consumption of 11-hydroperoxyoctadecadienoate to a ratio of 2/84/14. The (9E,11Z,15E)-octadeca-9,11,15-trienoic acid is transformed to 11- and (13R)-hydroperoxyoctadecatrienoic acid and to traces of (9S)-hydroperoxyoctadecatrienoic acid, essentially as native 13R-MnLOX
F347L
-
site-directed mutagenesis, (9E,11Z,15E)-octadeca-9,11,15-trienoic acid is oxidized to a 2:3 mixture of (9S)- and (13R)-dihydroxyoctadecatrienoic acid
F347V
-
site-directed mutagenesis
G316T
catalytically inactive
G316V
catalytically inactive
G332A
-
site-directed mutagenesis, replacement of Gly332 with the larger hydrophobic residue selectively augments dehydration of (9Z,11E,13R,15Z)-13-hydroperoxyoctadeca-9,12,15-trienoic acid and increases the oxidation at C-13 of 18:1n-6
H274Q
-
no enzymic activity, loss of more than 95% of manganese content
H278E
-
no enzymic activity, loss of more than 95% of manganese content
H462E
-
no enzymic activity, loss of more than 95% of manganese content
H463Q
-
no significant change in activity
K52N
-
site-directed mutagenesis
L176K
-
site-directed mutagenesis
L336A
-
site-directed mutagenesis, replacement of Leu336 with the smaller hydrophobic residue shifts the oxygenation from C-13 toward C-9 with formation of 9S- and 9R-hydroperoxy metabolites of 18:2n-6 and 18:3n-3, the mutant shows highly reduced activity compared to the wild-type enzyme
L336F
-
site-directed mutagenesis, replacement of Leu336 with the larger hydrophobic residue selectively augments dehydration of (9Z,11E,13R,15Z)-13-hydroperoxyoctadeca-9,12,15-trienoic acid and increases the oxidation at C-13 of 18:1n-6, the mutant shows highly reduced activity compared to the wild-type enzyme
L336G
-
site-directed mutagenesis, replacement of Leu336 with the smaller hydrophobic residue shifts the oxygenation from C-13 toward C-9 with formation of 9S- and 9R-hydroperoxy metabolites of 18:2n-6 and 18:3n-3, the mutant shows highly reduced activity compared to the wild-type enzyme
L336V
-
site-directed mutagenesis, replacement of Leu336 with the smaller hydrophobic residue shifts the oxygenation from C-13 toward C-9 with formation of 9S- and 9R-hydroperoxy metabolites of 18:2n-6 and 18:3n-3, the mutant shows highly reduced activity compared to the wild-type enzyme
N466Q
-
no significant change in activity
Q467N
-
no significant change in activity
S469A
-
site-directed mutagenesis, the mutation hardly affects the bis-allylic hydroperoxide rearrangement, the mutant shows the same substrate profile as the wild-type enzyme
Y158C
-
site-directed mutagenesis
A300G
site-directed mutagenesis, structure comparison with wild-type enzyme, enantioselectivity towards formation of 9R- and 13S-hydroperoxyoctadeca-9,12-dienoate is increased compared to the wild-type enzyme
I296A
site-directed mutagenesis, structure comparison with wild-type enzyme, the stereospecificity of the mutant activity is inverted compared to the wild-type enzyme
L258V
site-directed mutagenesis, structure comparison with wild-type enzyme, the mutation only slightly affects the enzyme activity
L502V
site-directed mutagenesis, structure comparison with wild-type enzyme, enantioselectivity towards formation of 9R- and 13S-hydroperoxyoctadeca-9,12-dienoate is increased compared to the wild-type enzyme
L506V
site-directed mutagenesis, structure comparison with wild-type enzyme, the stereospecificity of the mutant activity is inverted compared to the wild-type enzyme
G316A
catalytically active, 7-8% of hydroperoxide isomerase activity
G316A
-
site-directed mutagenesis, the mutant changes the the position of lipoxygenation toward the carboxyl group of 20:2n-6 and 20:3n-3 and prevents the bis-allylic hydroperoxide of 20:3n-3 but not of 20:2n-6to interact with the catalytic metall
G316A
-
site-directed mutagenesis, the mutant MnIII-LO G316A oxygenates mainly 16:3n-3 at positions n-7 and n-6, 19:3n-3 at n-10, n-8, and n-6, and 20:3n-3 at n-10 and n-8
N466L
-
no significant change in activity
N466L
-
site-directed mutagenesis, the mutation hardly affects the bis-allylic hydroperoxide rearrangement
additional information
-
replacement of a single amino acid in the active site of LOXs can alter the product profile
additional information
-
V602 deletion mutant, no enzymic activity, loss of more than 95% of manganese content
additional information
-
hydrophobic replacements of Leu336 can modify the hydroperoxide configurations at C-9 with little effect on the R configuration at C-13 of the 18:2n-6 and 18:3n-3 metabolites
additional information
-
replacement Phe347 in 13R-MnLOX and changes the regiospecific oxidation of 18:2 n-6 in a consistent way, but the n-3 double bond of 18:3n-3 can reduce this effect. Mutations are designed to convert the pentamer motif to a hexamer motif to mimic FeLOX, but the mutants with the His-Val-Leu-Phe-Thr-His and His-Val-Leu-Phe-Gly-His motives are inactive, overview
additional information
modulating the cavity volume around the pentadiene system of linoleic acid shifts the product formation towards 9S-, 9R-, 13S- or 13R-hydroperoxides in correlation with the site of mutation, thus decreasing the amount of the bis-allylic 11R-hydroperoxide
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Koch, R.B.; Brumfiel, B.L.; Brumfiel, M.N.
Calcium requirement for lipoxygenase catalyzed linoleate oxidation
J. Am. Oil Chem. Soc.
48
532-538
1971
Glycine max, Phaseolus vulgaris
brenda
Su, C.; Oliw, E.H.
Manganese lipoxygenase. Purification and characterization
J. Biol. Chem.
273
13072-13079
1998
Gaeumannomyces graminis
brenda
Hamberg, M.; Su, C.; Oliw, E.
Manganese lipoxygenase. Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction
J. Biol. Chem.
273
13080-13088
1998
Gaeumannomyces graminis
brenda
Su, C.; Sahlin, M.; Oliw, E.H.
Manganese lipoxygenase has a mononuclear redox center
Adv. Exp. Med. Biol.
507
171-176
2002
Gaeumannomyces graminis
brenda
Cristea, M.; Engstrom, K.; Su, C.; Hornsten, L.; Oliw, E.H.
Expression of manganese lipoxygenase in Pichia pastoris and site-directed mutagenesis of putative metal ligands
Arch. Biochem. Biophys.
434
201-211
2005
Gaeumannomyces graminis
brenda
Oliw, E.H.; Cristea, M.; Hamberg, M.
Biosynthesis and isomerization of 11-hydroperoxylinoleates by manganese- and iron-dependent lipoxygenases
Lipids
39
319-323
2004
Gaeumannomyces graminis
brenda
Cristea, M.; Oliw, E.H.
A G316A mutation of manganese lipoxygenase augments hydroperoxide isomerase activity: mechanism of biosynthesis of epoxyalcohols
J. Biol. Chem.
281
17612-17623
2006
Gaeumannomyces graminis (Q8X151)
brenda
Cristea, M.; Oliw, E.H.
On the singular, dual, and multiple positional specificity of manganese lipoxygenase and its G316A mutant
J. Lipid Res.
48
890-903
2007
Gaeumannomyces graminis
brenda
Oliw, E.H.
Factors influencing the rearrangement of bis-allylic hydroperoxides by manganese lipoxygenase
J. Lipid Res.
49
420-428
2008
Gaeumannomyces graminis
brenda
Hoffmann, I.; Hamberg, M.; Lindh, R.; Oliw, E.H.
Novel insights into cyclooxygenases, linoleate diol synthases, and lipoxygenases from deuterium kinetic isotope effects and oxidation of substrate analogs
Biochim. Biophys. Acta
1821
1508-1517
2012
Glycine max
brenda
Wennman, A.; Jerneren, F.; Hamberg, M.; Oliw, E.H.
Catalytic convergence of manganese and iron lipoxygenases by replacement of a single amino acid
J. Biol. Chem.
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Gaeumannomyces graminis
brenda
Wennman, A.; Oliw, E.H.
Secretion of two novel enzymes, manganese 9S-lipoxygenase and epoxy alcohol synthase, by the rice pathogen Magnaporthe salvinii
J. Lipid Res.
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Gaeumannomyces graminis
brenda
Wennman, A.; Jerneren, F.; Magnuson, A.; Oliw, E.H.
Expression and characterization of manganese lipoxygenase of the rice blast fungus reveals prominent sequential lipoxygenation of alpha-linolenic acid
Arch. Biochem. Biophys.
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2015
Pyricularia oryzae (G4NAP4), Pyricularia oryzae
brenda
Wennman, A.; Magnuson, A.; Hamberg, M.; Oliw, E.H.
Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers
J. Lipid Res.
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2015
Colletotrichum gloeosporioides, Fusarium oxysporum
brenda
Newie, J.; Neumann, P.; Werner, M.; Mata, R.A.; Ficner, R.; Feussner, I.
Lipoxygenase 2 from Cyanothece sp. controls dioxygen insertion by steric shielding and substrate fixation
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Rippkaea orientalis PCC 8801 (B7JX99)
brenda