BRENDA - Enzyme Database show
show all sequences of 1.13.11.B6

A dual positional specific lipoxygenase functions in the generation of flavor compounds during climacteric ripening of apple

Schiller, D.; Contreras, C.; Vogt, J.; Dunemann, F.; Defilippi, B.G.; Beaudry, R.; Schwab, W.; Hortic. Res. 2, 15003-15015 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene LOX1a, RT-PCR and real-time quantitative PCR expression analysis, 22 putative LOX genes in apple, gene expression analysis throughout ripening reveals that only six LOXs are expressed in a ripening-dependent manner, overview. DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged or untagged LOX genes endoing for isozymes LOX1:Md:1a, L, X1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b, containing an enterokinase cleavage recognition site in the first case, in Saccharomyces cerevisiae strain INVSc1, recombinant expression of YFP-tagged enzyme; gene LOX2a, RT-PCR and real-time quantitative PCR expression analysis, 22 putative LOX genes in apple, gene expression analysis throughout ripening reveals that only six LOXs are expressed in a ripening-dependent manner, overview. DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged or untagged LOX genes endoing for isozymes LOX1:Md:1a, L, X1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b, containing an enterokinase cleavage recognition site in the first case, in Saccharomyces cerevisiae strain INVSc1, recombinant expression of YFP-tagged enzyme
Malus domestica
Engineering
Amino acid exchange
Commentary
Organism
G567A
site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation; site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
I566F
site-directed mutagenesis, inactive mutant
Malus domestica
I578L
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
L572I
site-directed mutagenesis, inactive mutant
Malus domestica
additional information
mutants Arg268Ala, Gly567Ala, Ile578Leu and Val582Phe show high substrate conversion rates of linoleate, linolenate and arachidonate (60%-100% of wild-type LOX1:Md:1a activity with linoleate). Substrate specificity of mutants, overview
Malus domestica
R268A
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
V582F
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
Malus domestica
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
not in chloroplasts; not in chloroplasts
Malus domestica
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + O2
Malus domestica
-
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
-
-
?
linoleate + O2
Malus domestica
-
9-hydroperoxy-10,12-octadecadienoate + 13-hydroperoxy-9,11-octadecadienoate
-
-
?
linolenate + O2
Malus domestica
-
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Malus domestica
S4UKU4
LOX2:Md:2a
-
Malus domestica
S4UL92
LOX1:Md:1a
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration; recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration
Malus domestica
Source Tissue
Source Tissue
Commentary
Organism
Textmining
fruit
expression analysis of isozymes; high expression level of isozyme MdLOX1a gene in stored apple fruit, expression analysis of isozymes
Malus domestica
-
additional information
no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development; no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development
Malus domestica
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + O2
-
742627
Malus domestica
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
?
linoleate + O2
-
742627
Malus domestica
9-hydroperoxy-10,12-octadecadienoate + 13-hydroperoxy-9,11-octadecadienoate
-
-
-
?
linolenate + O2
-
742627
Malus domestica
?
-
-
-
?
additional information
regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX
742627
Malus domestica
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 101500, recombinant His-tagged isozyme LOX1a, SDS-PAGE; x * 106500, recombinant His-tagged isozyme LOX2a, SDS-PAGE
Malus domestica
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Malus domestica
45
-
-
Malus domestica
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
45
isozyme LOX2:Md:2a shows negligible activity at temperatures higher than 45°C
Malus domestica
15
55
isozyme LOX1:Md:1a shows a rather narrow optimum at 45°C with rapidly decreasing activity at lower or higher temperatures, but high residual activity at 55°C
Malus domestica
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Malus domestica
7
-
-
Malus domestica
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4.5
8
over 60% of maxmal activity within this range
Malus domestica
5
7.5
over 80% of maximal activity in a broad pH range with sharply decreasing relative activity below pH 5.0 and above pH 7.5
Malus domestica
Cloned(Commentary) (protein specific)
Commentary
Organism
gene LOX1a, RT-PCR and real-time quantitative PCR expression analysis, 22 putative LOX genes in apple, gene expression analysis throughout ripening reveals that only six LOXs are expressed in a ripening-dependent manner, overview. DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged or untagged LOX genes endoing for isozymes LOX1:Md:1a, L, X1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b, containing an enterokinase cleavage recognition site in the first case, in Saccharomyces cerevisiae strain INVSc1, recombinant expression of YFP-tagged enzyme
Malus domestica
gene LOX2a, RT-PCR and real-time quantitative PCR expression analysis, 22 putative LOX genes in apple, gene expression analysis throughout ripening reveals that only six LOXs are expressed in a ripening-dependent manner, overview. DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His-tagged or untagged LOX genes endoing for isozymes LOX1:Md:1a, L, X1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b, containing an enterokinase cleavage recognition site in the first case, in Saccharomyces cerevisiae strain INVSc1, recombinant expression of YFP-tagged enzyme
Malus domestica
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
G567A
site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
G567A
site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation
Malus domestica
I566F
site-directed mutagenesis, inactive mutant
Malus domestica
I578L
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
L572I
site-directed mutagenesis, inactive mutant
Malus domestica
additional information
mutants Arg268Ala, Gly567Ala, Ile578Leu and Val582Phe show high substrate conversion rates of linoleate, linolenate and arachidonate (60%-100% of wild-type LOX1:Md:1a activity with linoleate). Substrate specificity of mutants, overview
Malus domestica
R268A
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
V582F
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis
Malus domestica
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Malus domestica
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
additional information
not in chloroplasts
Malus domestica
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + O2
Malus domestica
-
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
-
-
?
linoleate + O2
Malus domestica
-
9-hydroperoxy-10,12-octadecadienoate + 13-hydroperoxy-9,11-octadecadienoate
-
-
?
linolenate + O2
Malus domestica
-
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration
Malus domestica
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
fruit
high expression level of isozyme MdLOX1a gene in stored apple fruit, expression analysis of isozymes
Malus domestica
-
fruit
expression analysis of isozymes
Malus domestica
-
additional information
no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development
Malus domestica
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + O2
-
742627
Malus domestica
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
-
-
-
?
linoleate + O2
-
742627
Malus domestica
9-hydroperoxy-10,12-octadecadienoate + 13-hydroperoxy-9,11-octadecadienoate
-
-
-
?
linolenate + O2
-
742627
Malus domestica
?
-
-
-
?
additional information
regio- and stereospecificity analysis of isozyme substrate specificity, recombinant LOX1:Md:1a, LOX1:Md:1c, LOX2:Md:2a and LOX2:Md:2b isozymes show 13/9-LOX, 9-LOX, 13/9-LOX and 13-LOX activity with linoleic acid, respectively. While products of LOX1:Md:1c and LOX2:Md:2b are S-configured, LOX1:Md:1a and LOX2:Md:2a form 13(R)-hydroperoxides as major products. Oxygenation in the carbon backbone of linoleic acid occurs either at carbon atom 9 (9-LOX) or 13 (13-LOX), forming the corresponding hydroperoxy derivatives, respectively. LOX enzymes are not perfectly specific and biocatalysts that produce more than 10% of the alternative regio-isomer are called dual positional specific LOX
742627
Malus domestica
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 101500, recombinant His-tagged isozyme LOX1a, SDS-PAGE
Malus domestica
?
x * 106500, recombinant His-tagged isozyme LOX2a, SDS-PAGE
Malus domestica
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
35
-
-
Malus domestica
45
-
-
Malus domestica
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
15
45
isozyme LOX2:Md:2a shows negligible activity at temperatures higher than 45°C
Malus domestica
15
55
isozyme LOX1:Md:1a shows a rather narrow optimum at 45°C with rapidly decreasing activity at lower or higher temperatures, but high residual activity at 55°C
Malus domestica
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Malus domestica
7
-
-
Malus domestica
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4.5
8
over 60% of maxmal activity within this range
Malus domestica
5
7.5
over 80% of maximal activity in a broad pH range with sharply decreasing relative activity below pH 5.0 and above pH 7.5
Malus domestica
General Information
General Information
Commentary
Organism
evolution
DNA and amino acid sequence determination and analysis of LOX1 and LOX2 isozymes, phylogenetic analysis, only LOX1:Md:1a exhibits a glycine residue (Gly567) responsible for dual positional specificity and (R)-LOX activity; DNA and amino acid sequence determination and analysis of LOX1 and LOX2 isozymes, phylogenetic analysis, only LOX1:Md:1a exhibits a glycine residue (Gly567) responsible for dual positional specificity and (R)-LOX activity
Malus domestica
metabolism
the enzyme is involved in the LOX pathway, overview; the enzyme is involved in the LOX pathway, overview
Malus domestica
additional information
structure homology modeling
Malus domestica
physiological function
lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus3domestica) fruit upon tissue disruption, role in autonomously produced aroma volatiles from intact tissue, overview. The genetic association with a quantitative trait locus for fruit ester and the remarkable agreement in regio- and stereoselectivity of the LOX1:Md:1a reaction with the overall LOX activity found in mature apple fruits, suggest a major physiological function of LOX1:Md:1a during climacteric ripening of apples. While isozymes LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b may contribute to aldehyde production in immature fruit upon cell disruption isozyme, LOX1:Md:1a probably regulates the availability of precursors for ester production in intact fruit tissue. Both 9- and 13-hydroperoxides can be catabolized to aroma-active volatile aldehydes by hydroperoxide lyase. Only 13-LOX activity contributes to the apple aroma due to the formation of precursors of C6 volatile compounds. The dioxygenation of PUFAs by 9- and 13-LOX activity forms precursors for important phytooxylipins with functions in plant defense, wound signaling, senescence and fruit ripening; lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus3domestica) fruit upon tissue disruption, role in autonomously produced aroma volatiles from intact tissue, overview. The genetic association with a quantitative trait locus for fruit ester and the remarkable agreement in regio- and stereoselectivity of the LOX1:Md:1a reaction with the overall LOX activity found in mature apple fruits, suggest a major physiological function of LOX1:Md:1a during climacteric ripening of apples. While isozymes LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b may contribute to aldehyde production in immature fruit upon cell disruption isozyme, LOX1:Md:1a probably regulates the availability of precursors for ester production in intact fruit tissue. Both 9- and 13-hydroperoxides can be catabolized to aroma-active volatile aldehydes by hydroperoxide lyase. Only 13-LOX activity contributes to the apple aroma due to the formation of precursors of C6 volatile compounds. The dioxygenation of PUFAs by 9- and 13-LOX activity forms precursors for important phytooxylipins with functions in plant defense, wound signaling, senescence and fruit ripening
Malus domestica
General Information (protein specific)
General Information
Commentary
Organism
evolution
DNA and amino acid sequence determination and analysis of LOX1 and LOX2 isozymes, phylogenetic analysis, only LOX1:Md:1a exhibits a glycine residue (Gly567) responsible for dual positional specificity and (R)-LOX activity
Malus domestica
metabolism
the enzyme is involved in the LOX pathway, overview
Malus domestica
additional information
structure homology modeling
Malus domestica
physiological function
lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus3domestica) fruit upon tissue disruption, role in autonomously produced aroma volatiles from intact tissue, overview. The genetic association with a quantitative trait locus for fruit ester and the remarkable agreement in regio- and stereoselectivity of the LOX1:Md:1a reaction with the overall LOX activity found in mature apple fruits, suggest a major physiological function of LOX1:Md:1a during climacteric ripening of apples. While isozymes LOX1:Md:1c, LOX2:Md:2a, and LOX2:Md:2b may contribute to aldehyde production in immature fruit upon cell disruption isozyme, LOX1:Md:1a probably regulates the availability of precursors for ester production in intact fruit tissue. Both 9- and 13-hydroperoxides can be catabolized to aroma-active volatile aldehydes by hydroperoxide lyase. Only 13-LOX activity contributes to the apple aroma due to the formation of precursors of C6 volatile compounds. The dioxygenation of PUFAs by 9- and 13-LOX activity forms precursors for important phytooxylipins with functions in plant defense, wound signaling, senescence and fruit ripening
Malus domestica
Other publictions for EC 1.13.11.B6
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)
742627
Schiller
A dual positional specific li ...
Malus domestica
Hortic. Res.
2
15003-15015
2015
-
-
1
-
7
-
-
1
1
-
-
4
-
4
-
-
1
-
-
2
-
-
6
1
2
2
-
-
2
2
-
-
-
-
-
-
-
2
-
-
8
-
-
-
-
2
2
-
-
4
-
-
-
2
-
4
-
-
6
2
2
2
-
-
2
2
-
-
-
4
7
-
-
-
725658
Wennman
Secretion of two novel enzymes ...
Nakataea oryzae, Nakataea oryzae CBS 288.54
J. Lipid Res.
54
762-775
2013
-
-
1
-
2
1
-
1
1
3
1
-
-
5
-
-
1
-
-
1
-
1
8
1
1
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
2
1
-
-
-
1
1
3
1
-
-
-
-
1
-
1
-
1
8
1
1
-
-
1
1
-
-
-
-
2
2
-
1
1
725856
Jerneren
Linolenate 9R-dioxygenase and ...
Lasiodiplodia theobromae, Lasiodiplodia theobromae 2334, Lasiodiplodia theobromae CBS 117454, Lasiodiplodia theobromae CBS 122127
Lipids
47
65-73
2012
-
-
-
-
-
-
-
-
1
-
-
13
-
6
-
-
-
-
-
1
-
-
17
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
13
-
-
-
-
-
1
-
-
17
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
724736
Chechetkin
Oxidation of glycerolipids by ...
Zea mays
Chem. Phys. Lipids
164
216-220
2011
-
-
1
-
1
-
-
-
-
-
-
3
-
2
-
-
-
-
-
-
-
-
12
-
-
-
-
-
1
-
-
-
-
-
-
-
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1
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
12
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
702431
Palmieri-Thiers
A lipoxygenase with dual posit ...
Olea europaea
Biochim. Biophys. Acta
1791
339-346
2009
-
-
1
-
-
-
2
2
1
-
2
-
-
1
-
-
1
-
-
1
1
-
2
1
-
-
-
2
1
-
-
-
2
1
-
-
-
1
-
-
-
-
-
2
2
2
1
-
2
-
-
-
-
1
-
1
1
-
2
1
-
-
-
2
1
-
-
1
-
1
1
-
2
2
706122
Hornung
Identification of an amino aci ...
Momordica charantia
Phytochemistry
69
2774-2780
2008
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
706252
Wang
A novel lipoxygenase gene from ...
Oryza sativa
Plant Mol. Biol.
66
401-414
2008
-
-
1
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2
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674388
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1
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706289
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A novel lipoxygenase in pea ro ...
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2006
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1
1
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3
1
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1
1
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703538
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706251
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Dual positional specificity an ...
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1
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396190
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703535
Hughes
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8
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1
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706250
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A peanut seed lipoxygenase res ...
Arachis hypogaea
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1
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4
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4
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3
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Skrzypczak-Jankun
Structure of soybean lipoxygen ...
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Soybean lipoxygenase-1 enzymic ...
Glycine max
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274-281
1989
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