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show all sequences of 5.4.4.6

Characterization of a recombinant 7,8-linoleate diol synthase from Glomerella cingulate

Seo, M.J.; Shin, K.C.; An, J.U.; Kang, W.R.; Ko, Y.J.; Oh, D.K.; Appl. Microbiol. Biotechnol. 100, 3087-3099 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
phylogenetic tree, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain ER2566
Colletotrichum gloeosporioides
Engineering
Amino acid exchange
Commentary
Organism
A891G
site-directed mutagenesis
Colletotrichum gloeosporioides
C1038S
site-directed mutagenesis
Colletotrichum gloeosporioides
H1036A
site-directed mutagenesis
Colletotrichum gloeosporioides
H1036A/C1038S
site-directed mutagenesis
Colletotrichum gloeosporioides
additional information
comparison of substrate specificities of wild-type and mutant enzymes, overview
Colletotrichum gloeosporioides
N895D
site-directed mutagenesis
Colletotrichum gloeosporioides
N895L
site-directed mutagenesis
Colletotrichum gloeosporioides
N895Q
site-directed mutagenesis
Colletotrichum gloeosporioides
Q898E
site-directed mutagenesis
Colletotrichum gloeosporioides
Q898L
site-directed mutagenesis
Colletotrichum gloeosporioides
Y380F
site-directed mutagenesis
Colletotrichum gloeosporioides
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0223
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
0.0333
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
0.0371
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
0.048
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
510000
-
recombinant enzyme, gel filtration
Colletotrichum gloeosporioides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Colletotrichum gloeosporioides
-
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Colletotrichum gloeosporioides
A0A0S2SWE4
i.e. Colletotrichum gloeosporioides
-
Colletotrichum gloeosporioides KACC 40961
A0A0S2SWE4
i.e. Colletotrichum gloeosporioides
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes 8fold from Escherichia coli strain ER2566 by nickel affinity chromatography
Colletotrichum gloeosporioides
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Colletotrichum gloeosporioides
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.39
-
purified recombinant enzyme, whole enzyme activity, substrate palmitoleate, pH 6.5, 40C
Colletotrichum gloeosporioides
0.48
-
purified recombinant enzyme, whole enzyme activity, substrate oleate, pH 6.5, 40C
Colletotrichum gloeosporioides
0.75
-
purified recombinant enzyme, whole enzyme activity, substrate alpha-linolenate, pH 6.5, 40C
Colletotrichum gloeosporioides
0.87
-
purified recombinant enzyme, whole enzyme activity, substrate (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, pH 6.5, 40C
Colletotrichum gloeosporioides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
741712
Colletotrichum gloeosporioides
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
r
alpha-linolenate + O2
via (9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoic acid, best substrate with respect to whole enzyme activity
741712
Colletotrichum gloeosporioides
(9Z,12Z,15Z)-7,8-dihydroperoxyoctadeca-9,12,15-trienoic acid
-
-
-
?
additional information
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via 8-hydroperoxy-9,12(Z,Z)-octadecadienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5S,8R,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
741712
Colletotrichum gloeosporioides
?
-
-
-
-
oleate + O2
via (9Z)-8-hydroperoxyoctadeca-9-enoic acid
741712
Colletotrichum gloeosporioides
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
-
-
-
?
palmitoleate + O2
via (9Z)-8-dihydroperoxyhexadeca-9-enoate
741712
Colletotrichum gloeosporioides
(9Z)-5,8-dihydroxyhexadeca-9-enoic acid
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 127000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 127413, sequence calculation
Colletotrichum gloeosporioides
More
the enzyme diol synthase is a fusion protein, consisting of an N-terminal dioxygenase domain and a C-terminal cytochrome P450/hydroperoxide isomerase domain
Colletotrichum gloeosporioides
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
whole enzyme activity
Colletotrichum gloeosporioides
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.86
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
5.62
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
6.58
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
10.5
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the maximum activity for the conversion of linoleic acid to (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) by 8-dioxygenase in the N-terminal domain of 7,8-LDS is observed at pH 7.0 and 20C, whereas that for the conversion of linoleic acid to (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by the whole enzyme is observed at pH 6.5 and 40C
Colletotrichum gloeosporioides
6.5
-
whole enzyme activity
Colletotrichum gloeosporioides
Cloned(Commentary) (protein specific)
Commentary
Organism
phylogenetic tree, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain ER2566
Colletotrichum gloeosporioides
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A891G
site-directed mutagenesis
Colletotrichum gloeosporioides
C1038S
site-directed mutagenesis
Colletotrichum gloeosporioides
H1036A
site-directed mutagenesis
Colletotrichum gloeosporioides
H1036A/C1038S
site-directed mutagenesis
Colletotrichum gloeosporioides
additional information
comparison of substrate specificities of wild-type and mutant enzymes, overview
Colletotrichum gloeosporioides
N895D
site-directed mutagenesis
Colletotrichum gloeosporioides
N895L
site-directed mutagenesis
Colletotrichum gloeosporioides
N895Q
site-directed mutagenesis
Colletotrichum gloeosporioides
Q898E
site-directed mutagenesis
Colletotrichum gloeosporioides
Q898L
site-directed mutagenesis
Colletotrichum gloeosporioides
Y380F
site-directed mutagenesis
Colletotrichum gloeosporioides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0223
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
0.0333
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
0.0371
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
0.048
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
510000
-
recombinant enzyme, gel filtration
Colletotrichum gloeosporioides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Colletotrichum gloeosporioides
-
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes 8fold from Escherichia coli strain ER2566 by nickel affinity chromatography
Colletotrichum gloeosporioides
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Colletotrichum gloeosporioides
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.39
-
purified recombinant enzyme, whole enzyme activity, substrate palmitoleate, pH 6.5, 40C
Colletotrichum gloeosporioides
0.48
-
purified recombinant enzyme, whole enzyme activity, substrate oleate, pH 6.5, 40C
Colletotrichum gloeosporioides
0.75
-
purified recombinant enzyme, whole enzyme activity, substrate alpha-linolenate, pH 6.5, 40C
Colletotrichum gloeosporioides
0.87
-
purified recombinant enzyme, whole enzyme activity, substrate (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, pH 6.5, 40C
Colletotrichum gloeosporioides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
741712
Colletotrichum gloeosporioides
(7S,8S,9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoate
-
-
-
r
alpha-linolenate + O2
via (9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoic acid, best substrate with respect to whole enzyme activity
741712
Colletotrichum gloeosporioides
(9Z,12Z,15Z)-7,8-dihydroperoxyoctadeca-9,12,15-trienoic acid
-
-
-
?
additional information
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via 8-hydroperoxy-9,12(Z,Z)-octadecadienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (7S,8S,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5S,8R,9Z,12Z)-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
741712
Colletotrichum gloeosporioides
?
-
-
-
-
oleate + O2
via (9Z)-8-hydroperoxyoctadeca-9-enoic acid
741712
Colletotrichum gloeosporioides
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
-
-
-
?
palmitoleate + O2
via (9Z)-8-dihydroperoxyhexadeca-9-enoate
741712
Colletotrichum gloeosporioides
(9Z)-5,8-dihydroxyhexadeca-9-enoic acid
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 127000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 127413, sequence calculation
Colletotrichum gloeosporioides
More
the enzyme diol synthase is a fusion protein, consisting of an N-terminal dioxygenase domain and a C-terminal cytochrome P450/hydroperoxide isomerase domain
Colletotrichum gloeosporioides
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
whole enzyme activity
Colletotrichum gloeosporioides
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.86
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
5.62
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
6.58
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
10.5
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the maximum activity for the conversion of linoleic acid to (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) by 8-dioxygenase in the N-terminal domain of 7,8-LDS is observed at pH 7.0 and 20C, whereas that for the conversion of linoleic acid to (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by the whole enzyme is observed at pH 6.5 and 40C
Colletotrichum gloeosporioides
6.5
-
whole enzyme activity
Colletotrichum gloeosporioides
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
8.125
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
14.41
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
23.45
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
33.62
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
8.125
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
14.41
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
23.45
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
33.62
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40C
Colletotrichum gloeosporioides
Other publictions for EC 5.4.4.6
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
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
-
11
-
-
4
-
-
1
1
-
3
-
-
1
-
-
1
4
-
5
2
1
-
-
4
2
-
-
-
-
-
-
-
-
1
-
-
11
-
-
-
-
4
-
-
1
1
-
-
-
1
-
1
4
-
5
2
1
-
-
4
2
-
-
-
-
-
-
-
4
4
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
-
3
-
-
1
-
-
1
-
-
8
-
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
8
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
702018
Garscha
Pichia expression and mutagene ...
Gaeumannomyces graminis, Gaeumannomyces graminis var. avenae
Biochem. Biophys. Res. Commun.
373
579-583
2008
-
-
1
-
3
-
-
-
-
-
-
4
-
4
-
1
1
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
4
-
-
-
-
-
-
-
-
4
-
-
2
2
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
703700
Garscha
Critical amino acids for the 8 ...
Gaeumannomyces graminis
FEBS Lett.
582
3547-3551
2008
-
-
1
-
11
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
11
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285246
Hrnsten
Cloning of linoleate diol synt ...
Gaeumannomyces graminis
J. Biol. Chem.
274
28219-28224
1999
-
-
1
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
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285251
Oliw
Catalytic properties of linole ...
Gaeumannomyces graminis
Adv. Exp. Med. Biol.
469
679-685
1999
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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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285249
Su
Studies on linoleic acid 8R-di ...
Gaeumannomyces graminis
Lipids
30
43-50
1995
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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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285250
Hamberg
Sequential oxygenation of lino ...
Gaeumannomyces graminis, Gaeumannomyces graminis var.graminis
Arch. Biochem. Biophys.
309
77-80
1994
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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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