BRENDA - Enzyme Database show
show all sequences of 1.13.11.45

Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers

Wennman, A.; Magnuson, A.; Hamberg, M.; Oliw, E.H.; J. Lipid Res. 56, 1606-1615 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic tree of two LOX prototypes from different species, recombinant expression and secretion of wild-type and mutant enzymes in Pichia pastoris
Fusarium oxysporum
Engineering
Amino acid exchange
Commentary
Organism
L530R
site-directed mutagenesis
Fusarium oxysporum
additional information
replacement of a single amino acid in the active site of LOXs can alter the product profile
Fusarium oxysporum
S348F
site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme
Fusarium oxysporum
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
enzyme-bound
Colletotrichum gloeosporioides
Cu2+
enzyme-bound, inhibits linoleate oxidation
Fusarium oxysporum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Colletotrichum gloeosporioides
additional information
-
additional information
Michaelis-Menten kinetics
Fusarium oxysporum
0.0106
-
(11Z,14Z)-eicosa-11,14-dienoic acid
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
0.0112
-
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
0.0122
-
linolenate
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Fusarium oxysporum
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
enzyme-bound
Colletotrichum gloeosporioides
Fe2+
enzyme-bound
Fusarium oxysporum
Mn2+
enzyme-bound, has catalytic function
Colletotrichum gloeosporioides
Mn2+
enzyme-bound, has catalytic function, but does not activate the enzyme exogenously
Fusarium oxysporum
additional information
determination of metal contents by EPR analysis
Colletotrichum gloeosporioides
additional information
determination of metal contents by EPR analysis
Fusarium oxysporum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Colletotrichum gloeosporioides
-
-
-
Fusarium oxysporum
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant secreted wild-type and mutant enzymes from Pichia pastoris by hydrophobic interaction chromatography, ultrafiltration, and gel filtration
Fusarium oxysporum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(11Z,14Z)-eicosa-11,14-dienoic acid + O2
LC-MS analysis shows that Fo-MnLOX oxidizes (11Z,14Z)-eicosa-11,14-dienoic acid efficiently at both C-15 and C-11
743055
Fusarium oxysporum
?
-
-
-
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
-
743055
Fusarium oxysporum
?
-
-
-
?
1-linoleoyl-2-lyso-phosphatidylcholine + O2
-
743055
Fusarium oxysporum
?
-
-
-
?
linolenate + O2
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
743055
Fusarium oxysporum
(11R)-hydroperoxyoctadecadienoic acid + 13 S-hydroperoxyoctadecadienoic acid + 9(S/R)-hydroperoxyoctadecadienoic acid
-
-
-
?
linolenate + O2
-
743055
Fusarium oxysporum
(11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
-
-
-
-
linolenate + O2 +
-
743055
Colletotrichum gloeosporioides
(11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
-
-
-
?
lyso-phosphatidylcholine + O2
substrate from soybean
743055
Colletotrichum gloeosporioides
?
-
-
-
?
lyso-phosphatidylcholine + O2
substrate from soybean
743055
Fusarium oxysporum
?
-
-
-
?
additional information
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
743055
Fusarium oxysporum
?
-
-
-
-
additional information
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
743055
Colletotrichum gloeosporioides
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0122
-
linolenate
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Fusarium oxysporum
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, phylogenetic tree of two LOX prototypes from different species, recombinant expression and secretion of wild-type and mutant enzymes in Pichia pastoris
Fusarium oxysporum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
L530R
site-directed mutagenesis
Fusarium oxysporum
additional information
replacement of a single amino acid in the active site of LOXs can alter the product profile
Fusarium oxysporum
S348F
site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme
Fusarium oxysporum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
enzyme-bound
Colletotrichum gloeosporioides
Cu2+
enzyme-bound, inhibits linoleate oxidation
Fusarium oxysporum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Colletotrichum gloeosporioides
additional information
-
additional information
Michaelis-Menten kinetics
Fusarium oxysporum
0.0106
-
(11Z,14Z)-eicosa-11,14-dienoic acid
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
0.0112
-
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
0.0122
-
linolenate
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
-
Fusarium oxysporum
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
enzyme-bound
Colletotrichum gloeosporioides
Fe2+
enzyme-bound
Fusarium oxysporum
Mn2+
enzyme-bound, has catalytic function
Colletotrichum gloeosporioides
Mn2+
enzyme-bound, has catalytic function, but does not activate the enzyme exogenously
Fusarium oxysporum
additional information
determination of metal contents by EPR analysis
Colletotrichum gloeosporioides
additional information
determination of metal contents by EPR analysis
Fusarium oxysporum
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant secreted wild-type and mutant enzymes from Pichia pastoris by hydrophobic interaction chromatography, ultrafiltration, and gel filtration
Fusarium oxysporum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(11Z,14Z)-eicosa-11,14-dienoic acid + O2
LC-MS analysis shows that Fo-MnLOX oxidizes (11Z,14Z)-eicosa-11,14-dienoic acid efficiently at both C-15 and C-11
743055
Fusarium oxysporum
?
-
-
-
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
-
743055
Fusarium oxysporum
?
-
-
-
?
1-linoleoyl-2-lyso-phosphatidylcholine + O2
-
743055
Fusarium oxysporum
?
-
-
-
?
linolenate + O2
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
743055
Fusarium oxysporum
(11R)-hydroperoxyoctadecadienoic acid + 13 S-hydroperoxyoctadecadienoic acid + 9(S/R)-hydroperoxyoctadecadienoic acid
-
-
-
?
linolenate + O2
-
743055
Fusarium oxysporum
(11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
-
-
-
-
linolenate + O2 +
-
743055
Colletotrichum gloeosporioides
(11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
-
-
-
?
lyso-phosphatidylcholine + O2
substrate from soybean
743055
Colletotrichum gloeosporioides
?
-
-
-
?
lyso-phosphatidylcholine + O2
substrate from soybean
743055
Fusarium oxysporum
?
-
-
-
?
additional information
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
743055
Fusarium oxysporum
?
-
-
-
-
additional information
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
743055
Colletotrichum gloeosporioides
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0122
-
linolenate
pH 9.0, temperature not specified in the publication, recombinant enzyme
Fusarium oxysporum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Fusarium oxysporum
General Information
General Information
Commentary
Organism
evolution
the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX
Fusarium oxysporum
additional information
structure-function analysis
Colletotrichum gloeosporioides
additional information
structure-function analysis
Fusarium oxysporum
General Information (protein specific)
General Information
Commentary
Organism
evolution
the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX
Fusarium oxysporum
additional information
structure-function analysis
Colletotrichum gloeosporioides
additional information
structure-function analysis
Fusarium oxysporum
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
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 ...
Cyanothece sp. PCC 8801
Sci. Rep.
7
2069
2017
-
-
1
1
6
-
-
-
-
1
-
1
-
2
-
-
1
1
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
6
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
741777
Wennman
Expression and characterizati ...
Magnaporthe oryzae, Magnaporthe oryzae 70-15
Arch. Biochem. Biophys.
583
87-95
2015
-
-
1
-
-
-
-
1
-
3
-
-
-
6
-
1
1
-
-
-
1
-
10
1
1
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
3
-
-
-
-
1
1
-
-
1
-
10
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
743055
Wennman
Manganese lipoxygenase of F. ...
Colletotrichum gloeosporioides, Fusarium oxysporum
J. Lipid Res.
56
1606-1615
2015
-
-
1
-
3
-
2
5
1
6
-
-
-
6
-
-
1
-
-
-
-
-
10
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
3
-
-
2
-
5
1
6
-
-
-
-
-
1
-
-
-
-
10
-
-
-
-
1
1
-
-
-
-
3
3
-
-
-
725658
Wennman
Secretion of two novel enzymes ...
Gaeumannomyces graminis
J. Lipid Res.
54
762-775
2013
-
-
1
-
4
1
-
-
-
1
-
-
-
4
-
-
1
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
4
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
724444
Hoffmann
Novel insights into cyclooxyge ...
Glycine max
Biochim. Biophys. Acta
1821
1508-1517
2012
-
-
-
-
-
-
-
-
-
1
-
-
-
3
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
725486
Wennman
Catalytic convergence of manga ...
Gaeumannomyces graminis
J. Biol. Chem.
287
31757-31765
2012
-
-
1
-
10
-
-
5
-
1
-
3
-
2
-
-
1
-
-
-
-
-
6
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
10
-
-
-
-
5
-
1
-
3
-
-
-
1
-
-
-
-
6
-
-
-
-
-
1
-
-
-
-
2
2
-
-
-
688235
Oliw
Factors influencing the rearra ...
Gaeumannomyces graminis
J. Lipid Res.
49
420-428
2008
-
-
1
-
3
-
-
1
1
2
-
-
-
1
-
-
-
1
-
-
-
-
9
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
688224
Cristea
On the singular, dual, and mul ...
Gaeumannomyces graminis
J. Lipid Res.
48
890-903
2007
-
-
1
-
1
-
-
-
-
1
-
-
-
1
-
-
1
1
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
674584
Cristea
A G316A mutation of manganese ...
Gaeumannomyces graminis
J. Biol. Chem.
281
17612-17623
2006
-
-
1
-
3
-
2
1
-
1
-
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
2
-
1
-
1
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654377
Cristea
Expression of manganese lipoxy ...
Gaeumannomyces graminis
Arch. Biochem. Biophys.
434
201-211
2005
-
-
-
-
8
-
-
1
-
1
-
-
-
5
-
1
-
-
-
1
1
1
1
1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
1
-
1
-
-
-
-
1
-
-
1
1
1
1
1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
656687
Oliw
Biosynthesis and isomerization ...
Gaeumannomyces graminis
Lipids
39
319-323
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654157
Su
Manganese lipoxygenase has a m ...
Gaeumannomyces graminis
Adv. Exp. Med. Biol.
507
171-176
2002
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285253
Su
Manganese lipoxygenase. Purifi ...
Gaeumannomyces graminis
J. Biol. Chem.
273
13072-13079
1998
-
-
-
-
-
-
4
3
-
1
3
-
-
1
-
1
1
-
-
-
-
1
3
-
1
1
1
3
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
3
-
1
3
-
-
-
1
1
-
-
-
1
3
-
1
1
1
3
1
1
-
-
-
-
-
-
-
-
285254
Hamberg
Manganese lipoxygenase. Discov ...
Gaeumannomyces graminis
J. Biol. Chem.
273
13080-13088
1998
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285252
Koch
Calcium requirement for lipoxy ...
Glycine max, Phaseolus vulgaris
J. Am. Oil Chem. Soc.
48
532-538
1971
-
-
-
-
-
-
1
-
-
4
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-