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Literature summary extracted from

  • Schiller, D.; Contreras, C.; Vogt, J.; Dunemann, F.; Defilippi, B.G.; Beaudry, R.; Schwab, W.
    A dual positional specific lipoxygenase functions in the generation of flavor compounds during climacteric ripening of apple (2015), Hortic. Res., 2, 15003-15015 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.11.B6 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
1.13.11.B6 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
1.13.11.12 gene LOX2b, 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 Malus domestica
1.13.11.58 gene LOX1c, 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 Malus domestica

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.B6 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
1.13.11.B6 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
1.13.11.B6 I566F site-directed mutagenesis, inactive mutant Malus domestica
1.13.11.B6 I578L site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis Malus domestica
1.13.11.B6 L572I site-directed mutagenesis, inactive mutant Malus domestica
1.13.11.B6 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
1.13.11.B6 R268A site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis Malus domestica
1.13.11.B6 V582F site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis Malus domestica
1.13.11.12 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
1.13.11.58 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.B6 additional information
-
additional information Michaelis-Menten kinetics Malus domestica
1.13.11.12 additional information
-
additional information Michaelis-Menten kinetics Malus domestica
1.13.11.58 additional information
-
additional information Michaelis-Menten kinetics Malus domestica

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.13.11.B6 additional information not in chloroplasts Malus domestica
-
-
1.13.11.12 additional information not in chloroplasts Malus domestica
-
-
1.13.11.58 additional information not in chloroplasts Malus domestica
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.B6 linoleate + O2 Malus domestica
-
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
-
?
1.13.11.B6 linoleate + O2 Malus domestica
-
9-hydroperoxy-10,12-octadecadienoate + 13-hydroperoxy-9,11-octadecadienoate
-
?
1.13.11.B6 linolenate + O2 Malus domestica
-
?
-
?
1.13.11.12 alpha-linolenate + O2 Malus domestica
-
13-hydroperoxyoctadeca-9,11,15-trienoate
-
?
1.13.11.12 linoleate + O2 Malus domestica
-
13-hydroperoxyoctadeca-9,11-dienoate
-
?
1.13.11.58 linoleate + O2 Malus domestica
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.B6 Malus domestica S4UKU4 LOX2:Md:2a
-
1.13.11.B6 Malus domestica S4UL92 LOX1:Md:1a
-
1.13.11.12 Malus domestica S4ULD7 LOX2:Md:2b
-
1.13.11.58 Malus domestica S4UL39 LOX2:Md:1c
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.B6 recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration Malus domestica
1.13.11.12 recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration Malus domestica
1.13.11.58 recombinant His-tagged enzymes from Saccharomyces cerevisiae strain INVSc1 by nickel affinity chromatographyand ultrafiltration Malus domestica

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.13.11.B6 fruit expression analysis of isozymes Malus domestica
-
1.13.11.B6 fruit high expression level of isozyme MdLOX1a gene in stored apple fruit, expression analysis of isozymes Malus domestica
-
1.13.11.B6 additional information no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development Malus domestica
-
1.13.11.12 fruit expression analysis of isozymes Malus domestica
-
1.13.11.12 additional information no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development Malus domestica
-
1.13.11.58 fruit expression analysis of isozymes Malus domestica
-
1.13.11.58 additional information no visible PCR bands from isozymes MdLOX1d, MdLOX4a, MdLOX5d, MdLOX5e and MdLOX9a during fruit development Malus domestica
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.B6 linoleate + O2
-
Malus domestica (9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
-
?
1.13.11.B6 linoleate + O2
-
Malus domestica 9-hydroperoxy-10,12-octadecadienoate + 13-hydroperoxy-9,11-octadecadienoate
-
?
1.13.11.B6 linolenate + O2
-
Malus domestica ?
-
?
1.13.11.B6 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 Malus domestica ?
-
?
1.13.11.12 alpha-linolenate + O2
-
Malus domestica 13-hydroperoxyoctadeca-9,11,15-trienoate
-
?
1.13.11.12 linoleate + O2
-
Malus domestica 13-hydroperoxyoctadeca-9,11-dienoate
-
?
1.13.11.12 linoleate + O2 the isozyme is specific for formation of the 13-H(p)ODE isomer (94%),very low 9-H(p)ODE activity (6%) Malus domestica 13-hydroperoxyoctadeca-9,11-dienoate
-
?
1.13.11.12 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 Malus domestica ?
-
?
1.13.11.58 linoleate + O2
-
Malus domestica (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
?
1.13.11.58 linoleate + O2 the enzyme specifically forms the 9-H(p)ODE isomer by 99.5%, 97.7% of which is in S-form Malus domestica (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
?
1.13.11.58 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 Malus domestica ?
-
?

Subunits

EC Number Subunits Comment Organism
1.13.11.B6 ? x * 101500, recombinant His-tagged isozyme LOX1a, SDS-PAGE Malus domestica
1.13.11.B6 ? x * 106500, recombinant His-tagged isozyme LOX2a, SDS-PAGE Malus domestica
1.13.11.12 ? x * 106600, recombinant His-tagged isozyme LOX2b, SDS-PAGE Malus domestica
1.13.11.58 ? x * 101600, recombinant His-tagged isozyme LOX1c, SDS-PAGE Malus domestica

Synonyms

EC Number Synonyms Comment Organism
1.13.11.B6 dual positional specific LOX
-
Malus domestica
1.13.11.B6 linoleate oxygen oxidoreductase
-
Malus domestica
1.13.11.B6 lipoxygenase
-
Malus domestica
1.13.11.B6 LOX
-
Malus domestica
1.13.11.B6 LOX1:Md:1a
-
Malus domestica
1.13.11.B6 LOX1a
-
Malus domestica
1.13.11.B6 LOX2:Md:2a
-
Malus domestica
1.13.11.B6 LOX2a
-
Malus domestica
1.13.11.12 linoleate oxygen oxidoreductase
-
Malus domestica
1.13.11.12 lipoxygenase
-
Malus domestica
1.13.11.12 LOX
-
Malus domestica
1.13.11.12 LOX2:Md:2b
-
Malus domestica
1.13.11.12 LOX2b
-
Malus domestica
1.13.11.12 type-2 13-LOX
-
Malus domestica
1.13.11.58 linoleate oxygen oxidoreductase
-
Malus domestica
1.13.11.58 lipoxygenase
-
Malus domestica
1.13.11.58 LOX
-
Malus domestica
1.13.11.58 LOX1:Md:1c
-
Malus domestica
1.13.11.58 LOX1c
-
Malus domestica
1.13.11.58 type-1 9-LOX
-
Malus domestica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.B6 35
-
-
Malus domestica
1.13.11.B6 45
-
-
Malus domestica
1.13.11.12 25
-
-
Malus domestica
1.13.11.58 45
-
-
Malus domestica

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.13.11.B6 15 45 isozyme LOX2:Md:2a shows negligible activity at temperatures higher than 45°C Malus domestica
1.13.11.B6 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
1.13.11.12 5 45 isozyme LOX2:Md:2b shows negligible activity at temperatures higher than 45°C, LOX2:Md:2b displays considerably high activity at 5°C with 60% of maximal activity Malus domestica
1.13.11.58 15 55 isozyme LOX1:Md:1c displays high catalytic activity in a broad range of temperatures between 15°C and 50°C, with a sharp decrease above 50°C Malus domestica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.11.B6 6
-
-
Malus domestica
1.13.11.B6 7
-
-
Malus domestica
1.13.11.12 7
-
-
Malus domestica
1.13.11.58 7.5
-
-
Malus domestica

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.13.11.B6 4.5 8 over 60% of maxmal activity within this range Malus domestica
1.13.11.B6 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
1.13.11.12 6 9.5 over 60% of maxmal activity within this range Malus domestica
1.13.11.58 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

EC Number General Information Comment Organism
1.13.11.B6 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
1.13.11.B6 metabolism the enzyme is involved in the LOX pathway, overview Malus domestica
1.13.11.B6 additional information structure homology modeling Malus domestica
1.13.11.B6 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
1.13.11.12 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
1.13.11.12 metabolism the enzyme is involved in the LOX pathway, overview Malus domestica
1.13.11.12 physiological function lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus domestica) 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
1.13.11.58 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
1.13.11.58 metabolism the enzyme is involved in the LOX pathway, overview Malus domestica
1.13.11.58 physiological function lipoxygenase (LOX) is an important contributor to the formation of aroma-active C6 aldehydes in apple (Malus domestica) 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