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Information on EC 1.13.11.60 - linoleate 8R-lipoxygenase and Organism(s) Gaeumannomyces graminis and UniProt Accession Q9UUS2
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1.13.11.60 linoleate 8R-lipoxygenaseIUBMB Comments
The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P-450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) . The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) .
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Word Map
- 1.13.11.60
- hydroperoxide
- graminis
-
gaeumannomyces
- oxylipins
-
dioxygenation
-
antarafacial
-
8r-hydroperoxylinoleic
-
allene
-
aspergilli
-
suprafacial
-
cyclooxygenases
-
ppoas
- verticillioides
-
take-all
-
homolytic
-
zymoseptoria
-
ferryl
- synthesis
The taxonomic range for the selected organisms is: Gaeumannomyces graminis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
linoleate diol synthase, 7,8-lds, 5,8-lds, 8r-dioxygenase, 8r-dox, 7,8-linoleate diol synthase, dioxygenase-cytochrome p450, 8(r)-dioxygenase, 8r-dox-5,8-lds, 5,8-linoleate diol synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7,8-LDS
7,8-linoleate diol synthase
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
linoleate:oxygen (8R)-oxidoreductase
The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P-450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) [1]. The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) [4].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-linolenic acid + O2
8(9)epoxy-10-hydroxy-(12Z,15Z)-octadecadienoate
-
-
-
?
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
-
-
-
?
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-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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the Ile and Trp conjugates of linoleate are not oxidized at C-8. The enzyme oxidizes the linoleate-Ile conjugate to 9- and 13-HODE-Ile and to 9(10)- and 12(13)epoxyalcohols. The alpha-linolenic acid-Ile conjugate is transformed to 9-, 13-, and 16-HOTrE-Ile in a ratio of 0.4:0.3:1, respectively
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
linoleate + O2
(8R,10E,12Z)-8-hydroperoxy-10,12-octadecadienoate
-
-
-
-
?
linoleate + O2
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heme
ferric hemeprotein. The proximal heme ligand of linoleate diol synthase is tentatively identified as His379 and the important tyrosine for catalysis as residue376 (apparent consensus EFNXXXYXWH). The distal heme ligand is tentatively identified as His203 (apparent consensus THXXFXT)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
linoleic acid
-
0.1 mM, partial inactivation, may indicate product inhibition
N-tosyl-L-phenylalanyl chloromethyl ketone
-
1 mM, over 70% inhibition
phenylmethanesulfonyl fluoride
-
0.2 mM, inhibits the 8R-dioxygenase enzyme by over 85%
N-[(E)-3-(3-phenoxyphenyl)prop-2-enyl]acetohydroxamic acid
-
i.e. BW A4C
N-[(E)-3-(3-phenoxyphenyl)prop-2-enyl]acetohydroxamic acid
i.e. BW A4C, more than 90% inhibition at 0.01 mM, about 50% inhibition at 0.001 mM
additional information
-
catalysis declines due to suicide inactivation
-
additional information
catalysis declines due to suicide inactivation
-
additional information
-
catalysis declines due to suicide inactivation. Following column chromatography, e.g. ion exchange or zinc-affinity chromatography, hydroperoxide isomerase activity is often decreased and sometimes even undetectable by TLC, whereas 8-dioxygenase activity is always present. However, storage of the enzyme for a few days on ice often restores the hydroperoxide isomerase and appeares to increase the 7,8-linoleate diol synthase activity as well
-
additional information
catalysis declines due to suicide inactivation. Following column chromatography, e.g. ion exchange or zinc-affinity chromatography, hydroperoxide isomerase activity is often decreased and sometimes even undetectable by TLC, whereas 8-dioxygenase activity is always present. However, storage of the enzyme for a few days on ice often restores the hydroperoxide isomerase and appeares to increase the 7,8-linoleate diol synthase activity as well
-
additional information
-
GSH (1 mM), GSSG (1 mM), EDTA (1 or 10 mM), EGTA (1 or 10 mM) and H202 (10 mM) are without effect on the 8R-dioxygenase
-
additional information
not inhibited by 1 mM KCN. CO does not inhibit the enzyme
-
additional information
-
sorbitol (0.75 M, 14%), glycerol (15%) and ethylene glycol (25%) do not inhibit the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic data of truncated enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
dithiothreitol
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
0.15
eicosatetraynoic acid
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
0.02
linoleate-hydroxamic acid
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
0.09
nordihydroguaiaretic acid
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
0.003 - 0.01
zileuton
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
0.0002
N-[(E)-3-(3-phenoxyphenyl)prop-2-enyl]acetohydroxamic acid
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
0.002
N-[(E)-3-(3-phenoxyphenyl)prop-2-enyl]acetohydroxamic acid
Gaeumannomyces graminis
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LIDS_GAEGR
1165
0
128322
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E384A
-
mutant forms only traces of (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
H379Q
N938D
-
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
-
site-directed mutagenesis, the mutation of the 7,8-linoleate diol synthase reduces the hydroperoxide isomerase activity of the enzyme
V330L
-
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
additional information
-
treatment with alpha-mannosidase to shorten N- and O-linked mannosides inhibis the hydroperoxide isomerase but not the 8(R)-dioxygenase
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
8R-dioxygenase is unstable during purification. It can be stabilized by glutathione, glutathione peroxidase and ethylenediaminetetraacetic acid
-
repeated freezing and thawing, particularly of dilute enzyme solutions, inactivates the enzyme
the enzyme is quite unstable at the early steps of purification, but active fractions from anion-exchange chromatography can be kept for 1 week on ice with only a small loss of enzyme activity
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
the enzyme can be incubated in 4 M urea for 1 h, followed by desalting, with only partial loss of enzyme activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Spodoptera frugiperda (Sf21) insect cells with native 8R-dioxygenase and hydroperoxide isomerase activities
expression in Pichia pastoris changes the position and stereospecificity of a hydroperoxide isomerase possibly due to N- or O-linked mannosides in the vicinity of the heme group, whereas the 8(R)-dioxygenase activity is identical with native 7,8-linoleate diol synthase
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Su, C.; Oliw, E.H.
Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as anovel hemoprotein
J. Biol. Chem.
271
14112-14118
1996
Gaeumannomyces graminis (Q9UUS2)
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)
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
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
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
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
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
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
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
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
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)
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
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
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
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