BRENDA - Enzyme Database
show all sequences of 1.13.11.45

Factors influencing the rearrangement of bis-allylic hydroperoxides by manganese lipoxygenase

Oliw, E.H.; J. Lipid Res. 49, 420-428 (2008) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Pichia pastoris
Gaeumannomyces graminis
Engineering
Protein Variants
Commentary
Organism
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
Gaeumannomyces graminis
N466L
site-directed mutagenesis, the mutation hardly affects the bis-allylic hydroperoxide rearrangement
Gaeumannomyces graminis
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
Gaeumannomyces graminis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0024
-
linoleate
pH 7.5, 18:3n-3 substrate
Gaeumannomyces graminis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
secretion
Gaeumannomyces graminis
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
required for activity
Gaeumannomyces graminis
additional information
no activity with Fe3+
Gaeumannomyces graminis
Organism
Organism
UniProt
Commentary
Textmining
Gaeumannomyces graminis
-
take-all fungus
-
Reaction
Reaction
Commentary
Organism
Reaction ID
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
reaction mechanism, tail-first model with rearrangement at C13 at the end of lipoxygenation, influenced by double bond configuration and the chain length of fatty acids, overview
Gaeumannomyces graminis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(11Z,14Z)-eicosadienoic acid + O2
-
688235
Gaeumannomyces graminis
15-hydroxyperoxy-(9Z,11E)-eicosadienoic acid
-
-
-
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
via 11-hydroperoxyoctadecadienoic acid, 13-hydroperoxyoctadecadienoic acid and 15-hydroperoxyoctadecadienoic acid
688235
Gaeumannomyces graminis
15-hydroxyperoxy-11Z,13E,17Z-eicosatrienoic acid
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
oxidation at the n-3 position
688235
Gaeumannomyces graminis
?
-
-
-
?
1-linoleyl-lyso-glycerophosphatidylcholine + O2
via formation of the 13-hydroxyperoxy metabolite
688235
Gaeumannomyces graminis
11-hydroxyoctadecanoic acid + 13-hydroxyoctadecanoic acid
-
-
-
?
11-hydroperoxyoctadecadienoic acid + O2
-
688235
Gaeumannomyces graminis
11,18-dihydroxy-12E,14Z,16E-eicosatrienoic acid
two diastereoisomers
-
-
?
alpha-linolenic acid + O2
-
688235
Gaeumannomyces graminis
(13R)-hydroperoxy octadecadienoic acid + 9-hydroperoxyoctadecadienoic acid
-
-
-
?
linoleate + O2
-
688235
Gaeumannomyces graminis
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleic acid + O2
-
688235
Gaeumannomyces graminis
?
-
-
-
?
additional information
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
688235
Gaeumannomyces graminis
?
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
manganese lipoxygenase
-
Gaeumannomyces graminis
Mn-LOX
-
Gaeumannomyces graminis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
40
-
linoleate
pH 7.5, 18:3n-3 substrate
Gaeumannomyces graminis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Gaeumannomyces graminis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Pichia pastoris
Gaeumannomyces graminis
Engineering (protein specific)
Protein Variants
Commentary
Organism
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
Gaeumannomyces graminis
N466L
site-directed mutagenesis, the mutation hardly affects the bis-allylic hydroperoxide rearrangement
Gaeumannomyces graminis
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
Gaeumannomyces graminis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0024
-
linoleate
pH 7.5, 18:3n-3 substrate
Gaeumannomyces graminis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
secretion
Gaeumannomyces graminis
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
required for activity
Gaeumannomyces graminis
additional information
no activity with Fe3+
Gaeumannomyces graminis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(11Z,14Z)-eicosadienoic acid + O2
-
688235
Gaeumannomyces graminis
15-hydroxyperoxy-(9Z,11E)-eicosadienoic acid
-
-
-
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
via 11-hydroperoxyoctadecadienoic acid, 13-hydroperoxyoctadecadienoic acid and 15-hydroperoxyoctadecadienoic acid
688235
Gaeumannomyces graminis
15-hydroxyperoxy-11Z,13E,17Z-eicosatrienoic acid
-
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
oxidation at the n-3 position
688235
Gaeumannomyces graminis
?
-
-
-
?
1-linoleyl-lyso-glycerophosphatidylcholine + O2
via formation of the 13-hydroxyperoxy metabolite
688235
Gaeumannomyces graminis
11-hydroxyoctadecanoic acid + 13-hydroxyoctadecanoic acid
-
-
-
?
11-hydroperoxyoctadecadienoic acid + O2
-
688235
Gaeumannomyces graminis
11,18-dihydroxy-12E,14Z,16E-eicosatrienoic acid
two diastereoisomers
-
-
?
alpha-linolenic acid + O2
-
688235
Gaeumannomyces graminis
(13R)-hydroperoxy octadecadienoic acid + 9-hydroperoxyoctadecadienoic acid
-
-
-
?
linoleate + O2
-
688235
Gaeumannomyces graminis
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleic acid + O2
-
688235
Gaeumannomyces graminis
?
-
-
-
?
additional information
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
688235
Gaeumannomyces graminis
?
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
40
-
linoleate
pH 7.5, 18:3n-3 substrate
Gaeumannomyces graminis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Gaeumannomyces graminis
Other publictions for EC 1.13.11.45
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)
743826
Newie
Lipoxygenase 2 from Cyanothec ...
Rippkaea orientalis PCC 8801
Sci. Rep.
7
2069
2017
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-
1
1
6
-
-
-
-
1
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1
-
5
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1
1
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2
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2
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1
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1
1
1
6
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1
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1
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1
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2
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1
1
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741777
Wennman
Expression and characterizati ...
Pyricularia oryzae
Arch. Biochem. Biophys.
583
87-95
2015
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1
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1
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3
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7
-
1
1
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1
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5
1
4
1
-
1
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1
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1
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1
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3
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1
1
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1
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5
1
1
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1
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1
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-
743055
Wennman
Manganese lipoxygenase of F. ...
Colletotrichum gloeosporioides, Fusarium oxysporum
J. Lipid Res.
56
1606-1615
2015
-
-
1
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3
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2
5
1
6
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12
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1
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10
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1
1
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3
3
-
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-
725658
Wennman
Secretion of two novel enzymes ...
Gaeumannomyces graminis
J. Lipid Res.
54
762-775
2013
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1
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4
1
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1
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6
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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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3
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1
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1
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-
2
2
-
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-
724444
Hoffmann
Novel insights into cyclooxyge ...
Glycine max
Biochim. Biophys. Acta
1821
1508-1517
2012
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1
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5
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3
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1
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1
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725486
Wennman
Catalytic convergence of manga ...
Gaeumannomyces graminis
J. Biol. Chem.
287
31757-31765
2012
-
-
1
-
10
-
-
5
-
1
-
3
-
2
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1
-
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6
-
1
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1
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1
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10
-
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5
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1
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3
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1
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6
-
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1
-
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-
2
2
-
-
-
688235
Oliw
Factors influencing the rearra ...
Gaeumannomyces graminis
J. Lipid Res.
49
420-428
2008
-
-
1
-
3
-
-
1
1
2
-
-
-
3
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1
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9
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2
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1
1
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1
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9
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1
1
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688224
Cristea
On the singular, dual, and mul ...
Gaeumannomyces graminis
J. Lipid Res.
48
890-903
2007
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1
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1
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2
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1
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10
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10
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674584
Cristea
A G316A mutation of manganese ...
Gaeumannomyces graminis
J. Biol. Chem.
281
17612-17623
2006
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1
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3
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1
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654377
Cristea
Expression of manganese lipoxy ...
Gaeumannomyces graminis
Arch. Biochem. Biophys.
434
201-211
2005
-
-
-
-
8
-
-
1
-
1
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7
-
1
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1
1
1
1
1
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8
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2
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656687
Oliw
Biosynthesis and isomerization ...
Gaeumannomyces graminis
Lipids
39
319-323
2004
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654157
Su
Manganese lipoxygenase has a m ...
Gaeumannomyces graminis
Adv. Exp. Med. Biol.
507
171-176
2002
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285253
Su
Manganese lipoxygenase. Purifi ...
Gaeumannomyces graminis
J. Biol. Chem.
273
13072-13079
1998
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3
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3
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1
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1
1
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285254
Hamberg
Manganese lipoxygenase. Discov ...
Gaeumannomyces graminis
J. Biol. Chem.
273
13080-13088
1998
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285252
Koch
Calcium requirement for lipoxy ...
Glycine max, Phaseolus vulgaris
J. Am. Oil Chem. Soc.
48
532-538
1971
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