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 |
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 |
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 |
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 | - |
- |
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 | - |
? |
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 | - |
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 |
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 | - |
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 | ? | - |
? |
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 |
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 |
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 |
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 |
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 |
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 |
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 |