BRENDA - Enzyme Database
show all sequences of 1.13.11.60

Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450

Brodhun, F.; Goebel, C.; Hornung, E.; Feussner, I.; J. Biol. Chem. 284, 11792-11805 (2009)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Aspergillus nidulans
Engineering
Protein Variants
Commentary
Organism
H1004A
mutant enzyme with abolished 8-hydroperoxide isomerase activity, whereas dioxygenase activity is still present
Aspergillus nidulans
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
Aspergillus nidulans
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
suicide inactivation, activity falls to zero within a few min although substrates were available in sufficient amounts
Aspergillus nidulans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.005
-
palmitoleate
pH 7.2, 24°C
Aspergillus nidulans
0.00671
-
oleate
pH 7.2, 24°C
Aspergillus nidulans
0.0183
-
linoleate
pH 7.2, 24°C
Aspergillus nidulans
0.0226
-
(11Z)-icos-11-enoic acid
pH 7.2, 24°C
Aspergillus nidulans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
110000
-
4 * 110000, SDS-PAGE
Aspergillus nidulans
440000
-
gel filtration
Aspergillus nidulans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
linoleate + O2
Aspergillus nidulans
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
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Aspergillus nidulans
Q6RET3
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Aspergillus nidulans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.2
-
pH 7.2, 24°C
Aspergillus nidulans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(11Z)-icos-11-enoic acid + O2
-
704466
Aspergillus nidulans
10-hydroperoxyeicosenoic acid
-
-
-
?
(11Z,14Z)-icosa-11,14-dienoic acid + O2
-
704466
Aspergillus nidulans
(11Z,14Z)-10-hydroperoxyeicosa-11,14-dienoic acid
-
-
-
?
(11Z,14Z,17Z)-icosa-11,14,17-trienoic acid + O2
-
704466
Aspergillus nidulans
(11Z,14Z,17Z)-10-hydroperoxyeicosa-11,14,17-trienoic acid
-
-
-
?
linoleate + O2
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
704466
Aspergillus nidulans
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
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
704466
Aspergillus nidulans
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
oleate + O2
-
704466
Aspergillus nidulans
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
palmitoleate + O2
-
704466
Aspergillus nidulans
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 110000, SDS-PAGE
Aspergillus nidulans
Synonyms
Synonyms
Commentary
Organism
PpoA
-
Aspergillus nidulans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
24
-
assay at
Aspergillus nidulans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.5
-
palmitoleate
pH 7.2, 24°C
Aspergillus nidulans
4.95
-
oleate
pH 7.2, 24°C
Aspergillus nidulans
5.9
-
(11Z)-icos-11-enoic acid
pH 7.2, 24°C
Aspergillus nidulans
6.3
-
linoleate
pH 7.2, 24°C
Aspergillus nidulans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Aspergillus nidulans
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
PpoA contains a high spin ferriheme. PpoA uses different heme domains to catalyze two separate reactions. Within the N-terminal heme peroxidase domain, linoleic acid is oxidized to (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate by abstracting a H-atom from C-8 of the fatty acid, yielding a carbon-centered radical that reacts with molecular dioxygen. In the second reaction step, (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate is isomerized within the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate
Aspergillus nidulans
heme
PpoA contains a high spin ferriheme. PpoA uses different heme domains to catalyze two separate reactions. Within the N-terminal heme peroxidase domain, linoleic acid is oxidized to (8R)-hydroperoxyoctadecadienoic acid by abstracting a H-atom from C-8 of the fatty acid, yielding a carbon-centered radical that reacts with molecular dioxygen. In the second reaction step, 8-hydroperoxyoctadecadienoic acid is isomerized within the C-terminal P450 heme thiolate domain to 5,8-dihydroxyoctadecadienoic acid
Aspergillus nidulans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Aspergillus nidulans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
PpoA contains a high spin ferriheme. PpoA uses different heme domains to catalyze two separate reactions. Within the N-terminal heme peroxidase domain, linoleic acid is oxidized to (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate by abstracting a H-atom from C-8 of the fatty acid, yielding a carbon-centered radical that reacts with molecular dioxygen. In the second reaction step, (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate is isomerized within the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxy-9,12-octadecadienoate
Aspergillus nidulans
heme
PpoA contains a high spin ferriheme. PpoA uses different heme domains to catalyze two separate reactions. Within the N-terminal heme peroxidase domain, linoleic acid is oxidized to (8R)-hydroperoxyoctadecadienoic acid by abstracting a H-atom from C-8 of the fatty acid, yielding a carbon-centered radical that reacts with molecular dioxygen. In the second reaction step, 8-hydroperoxyoctadecadienoic acid is isomerized within the C-terminal P450 heme thiolate domain to 5,8-dihydroxyoctadecadienoic acid
Aspergillus nidulans
Engineering (protein specific)
Protein Variants
Commentary
Organism
H1004A
mutant enzyme with abolished 8-hydroperoxide isomerase activity, whereas dioxygenase activity is still present
Aspergillus nidulans
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
Aspergillus nidulans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
suicide inactivation, activity falls to zero within a few min although substrates were available in sufficient amounts
Aspergillus nidulans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.005
-
palmitoleate
pH 7.2, 24°C
Aspergillus nidulans
0.00671
-
oleate
pH 7.2, 24°C
Aspergillus nidulans
0.0183
-
linoleate
pH 7.2, 24°C
Aspergillus nidulans
0.0226
-
(11Z)-icos-11-enoic acid
pH 7.2, 24°C
Aspergillus nidulans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
110000
-
4 * 110000, SDS-PAGE
Aspergillus nidulans
440000
-
gel filtration
Aspergillus nidulans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
linoleate + O2
Aspergillus nidulans
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
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Aspergillus nidulans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.2
-
pH 7.2, 24°C
Aspergillus nidulans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(11Z)-icos-11-enoic acid + O2
-
704466
Aspergillus nidulans
10-hydroperoxyeicosenoic acid
-
-
-
?
(11Z,14Z)-icosa-11,14-dienoic acid + O2
-
704466
Aspergillus nidulans
(11Z,14Z)-10-hydroperoxyeicosa-11,14-dienoic acid
-
-
-
?
(11Z,14Z,17Z)-icosa-11,14,17-trienoic acid + O2
-
704466
Aspergillus nidulans
(11Z,14Z,17Z)-10-hydroperoxyeicosa-11,14,17-trienoic acid
-
-
-
?
linoleate + O2
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
704466
Aspergillus nidulans
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
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
704466
Aspergillus nidulans
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
oleate + O2
-
704466
Aspergillus nidulans
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
palmitoleate + O2
-
704466
Aspergillus nidulans
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 110000, SDS-PAGE
Aspergillus nidulans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
24
-
assay at
Aspergillus nidulans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.5
-
palmitoleate
pH 7.2, 24°C
Aspergillus nidulans
4.95
-
oleate
pH 7.2, 24°C
Aspergillus nidulans
5.9
-
(11Z)-icos-11-enoic acid
pH 7.2, 24°C
Aspergillus nidulans
6.3
-
linoleate
pH 7.2, 24°C
Aspergillus nidulans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Aspergillus nidulans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
261
-
(11Z)-icos-11-enoic acid
pH 7.2, 24°C
Aspergillus nidulans
344
-
linoleate
pH 7.2, 24°C
Aspergillus nidulans
700
-
palmitoleate
pH 7.2, 24°C
Aspergillus nidulans
738
-
oleate
pH 7.2, 24°C
Aspergillus nidulans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
261
-
(11Z)-icos-11-enoic acid
pH 7.2, 24°C
Aspergillus nidulans
344
-
linoleate
pH 7.2, 24°C
Aspergillus nidulans
700
-
palmitoleate
pH 7.2, 24°C
Aspergillus nidulans
738
-
oleate
pH 7.2, 24°C
Aspergillus nidulans
Other publictions for EC 1.13.11.60
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741712
Seo
Characterization of a recombi ...
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides KACC 40961
Appl. Microbiol. Biotechnol.
100
3087-3099
2016
1
-
1
-
11
-
-
17
-
-
1
1
1
5
-
-
1
-
-
1
8
-
25
3
1
2
-
1
18
3
-
-
-
-
-
-
1
-
1
-
-
11
-
-
-
-
17
-
-
1
1
1
-
-
1
-
1
8
-
25
3
2
-
1
18
3
-
-
-
-
-
-
-
20
20
742730
Seo
Production of 7,8-dihydroxy u ...
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides KACC 40961
J. Agric. Food Chem.
64
8555-8562
2016
1
1
1
-
1
-
-
-
-
-
-
2
-
6
-
-
1
-
-
1
-
-
14
-
3
1
-
-
-
1
-
-
-
-
-
-
1
1
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
14
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
743200
Sooman
Discovery of a novel linoleat ...
Colletotrichum graminicola, Colletotrichum graminicola M1.001, Colletotrichum graminicola M1.001 / M2 / FGSC 10212, Fusarium oxysporum, Fusarium oxysporum Fo5176
Lipids
50
1243-1252
2015
-
-
1
-
-
-
-
-
-
-
-
5
-
13
-
-
-
-
-
-
-
-
29
-
8
2
2
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
29
-
2
2
-
-
-
-
-
-
-
2
2
-
-
-
724132
Hoffmann
7,8- and 5,8-linoleate diol sy ...
Aspergillus fumigatus, Gaeumannomyces graminis
Arch. Biochem. Biophys.
539
87-91
2013
-
-
2
-
7
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
5
2
4
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
711024
Hoffmann
Expression of 5,8-LDS of Asper ...
Aspergillus fumigatus, Gaeumannomyces graminis
Arch. Biochem. Biophys.
506
216-222
2010
-
-
2
-
6
-
-
2
-
-
-
3
-
4
-
-
-
-
-
2
-
-
10
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
7
-
-
-
-
2
-
-
-
3
-
-
-
-
-
2
-
-
10
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
714317
Jernerén
Reaction mechanism of 5,8-lino ...
Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
704466
Brodhun
Identification of PpoA from As ...
Aspergillus nidulans
J. Biol. Chem.
284
11792-11805
2009
-
-
1
-
2
-
1
4
-
-
2
1
-
1
-
-
1
-
-
-
1
-
7
1
1
1
-
-
4
1
-
-
2
-
-
-
-
-
1
2
-
2
-
-
1
-
4
-
-
2
1
-
-
-
1
-
-
1
-
7
1
1
-
-
4
1
-
-
-
-
-
-
-
4
4
704475
Garscha
Leucine/valine residues direct ...
Gaeumannomyces graminis
J. Biol. Chem.
284
13755-13765
2009
-
-
1
-
4
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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2
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702018
Garscha
Pichia expression and mutagene ...
Gaeumannomyces graminis, Gaeumannomyces graminis var. avenae
Biochem. Biophys. Res. Commun.
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579-583
2008
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3
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703700
Garscha
Critical amino acids for the 8 ...
Gaeumannomyces graminis
FEBS Lett.
582
3547-3551
2008
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1
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11
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1
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11
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1
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285246
Hörnsten
Cloning of linoleate diol synt ...
Gaeumannomyces graminis
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28219-28224
1999
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1
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1
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285251
Oliw
Catalytic properties of linole ...
Gaeumannomyces graminis
Adv. Exp. Med. Biol.
469
679-685
1999
2
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2
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1
1
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2
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1
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1
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1
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1
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285244
Su
A protein radical and ferryl i ...
Gaeumannomyces graminis
J. Biol. Chem.
273
20744-20751
1998
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1
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4
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1
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5
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1
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2
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2
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2
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5
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285243
Su
Purification and characterizat ...
Gaeumannomyces graminis
J. Biol. Chem.
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14112-14118
1996
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2
2
2
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2
1
1
1
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1
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1
1
1
2
1
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1
1
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1
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2
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2
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2
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2
1
1
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1
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1
1
1
2
1
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1
1
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1
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285249
Su
Studies on linoleic acid 8R-di ...
Gaeumannomyces graminis
Lipids
30
43-50
1995
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1
16
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1
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3
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1
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1
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1
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1
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1
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1
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16
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1
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1
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1
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1
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285247
Brodowsky
BW A4C and other hydroxamic ac ...
Gaeumannomyces graminis
Eur. J. Pharmacol.
254
43-47
1994
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12
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1
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1
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1
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1
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1
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6
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6
12
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1
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1
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1
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1
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1
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285248
Brodowsky
Linoleic acid 8R-dioxygenase a ...
Gaeumannomyces graminis
Ann. N. Y. Acad. Sci.
744
314-316
1994
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5
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1
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1
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5
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5
5
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1
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1
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285250
Hamberg
Sequential oxygenation of lino ...
Gaeumannomyces graminis
Arch. Biochem. Biophys.
309
77-80
1994
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2
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4
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285245
Brodowsky
A linoleic acid (8R)-dioxygena ...
Gaeumannomyces graminis
J. Biol. Chem.
267
14738-14745
1992
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1
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1
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