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Literature summary extracted from
- Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers (2015), J. Lipid Res., 56, 1606-1615 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.45 | 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 |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.45 | L530R | site-directed mutagenesis | Fusarium oxysporum |
| 1.13.11.45 | additional information | replacement of a single amino acid in the active site of LOXs can alter the product profile | Fusarium oxysporum |
| 1.13.11.45 | S348F | site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme | Fusarium oxysporum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.45 | Cu2+ | enzyme-bound | Colletotrichum gloeosporioides |  |
| 1.13.11.45 | Cu2+ | enzyme-bound, inhibits linoleate oxidation | Fusarium oxysporum | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.13.11.45 | additional information | - |
additional information | Michaelis-Menten kinetics | Colletotrichum gloeosporioides | |
| 1.13.11.45 | additional information | - |
additional information | Michaelis-Menten kinetics | Fusarium oxysporum | |
| 1.13.11.45 | 0.0106 | - |
(11Z,14Z)-eicosa-11,14-dienoic acid | pH 9.0, temperature not specified in the publication, recombinant enzyme | Fusarium oxysporum | |
| 1.13.11.45 | 0.0112 | - |
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid | pH 9.0, temperature not specified in the publication, recombinant enzyme | Fusarium oxysporum | |
| 1.13.11.45 | 0.0122 | - |
linolenate | pH 9.0, temperature not specified in the publication, recombinant enzyme | Fusarium oxysporum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.13.11.45 | extracellular | - |
Fusarium oxysporum | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.13.11.45 | Fe2+ | enzyme-bound | Colletotrichum gloeosporioides | |
| 1.13.11.45 | Fe2+ | enzyme-bound | Fusarium oxysporum | |
| 1.13.11.45 | Mn2+ | enzyme-bound, has catalytic function | Colletotrichum gloeosporioides | |
| 1.13.11.45 | Mn2+ | enzyme-bound, has catalytic function, but does not activate the enzyme exogenously | Fusarium oxysporum | |
| 1.13.11.45 | additional information | determination of metal contents by EPR analysis | Colletotrichum gloeosporioides | |
| 1.13.11.45 | additional information | determination of metal contents by EPR analysis | Fusarium oxysporum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.45 | Colletotrichum gloeosporioides | - |
- |
- |
| 1.13.11.45 | Fusarium oxysporum | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.11.45 | recombinant secreted wild-type and mutant enzymes from Pichia pastoris by hydrophobic interaction chromatography, ultrafiltration, and gel filtration | Fusarium oxysporum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.45 | (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 | Fusarium oxysporum | ? | - |
? | |
| 1.13.11.45 | (11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2 | - |
Fusarium oxysporum | ? | - |
? | |
| 1.13.11.45 | 1-linoleoyl-2-lyso-phosphatidylcholine + O2 | - |
Fusarium oxysporum | ? | - |
? | |
| 1.13.11.45 | linolenate + O2 | - |
Colletotrichum gloeosporioides | (11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid | - |
? | |
| 1.13.11.45 | 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 | Fusarium oxysporum | (11R)-hydroperoxyoctadecadienoic acid + 13S-hydroperoxyoctadecadienoic acid + 9(S/R)-hydroperoxyoctadecadienoic acid | - |
? | |
| 1.13.11.45 | lyso-phosphatidylcholine + O2 | substrate from soybean | Colletotrichum gloeosporioides | ? | - |
? | |
| 1.13.11.45 | lyso-phosphatidylcholine + O2 | substrate from soybean | Fusarium oxysporum | ? | - |
? | |
| 1.13.11.45 | 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 | Fusarium oxysporum | ? | - |
? | |
| 1.13.11.45 | 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 | Colletotrichum gloeosporioides | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.45 | Cg-MnLOX | - |
Colletotrichum gloeosporioides |
| 1.13.11.45 | Fo-MnLOX | - |
Fusarium oxysporum |
| 1.13.11.45 | manganese lipoxygenase | - |
Colletotrichum gloeosporioides |
| 1.13.11.45 | manganese lipoxygenase | - |
Fusarium oxysporum |
| 1.13.11.45 | manganese LOX | - |
Colletotrichum gloeosporioides |
| 1.13.11.45 | manganese LOX | - |
Fusarium oxysporum |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.13.11.45 | 0.0122 | - |
linolenate | pH 9.0, temperature not specified in the publication, recombinant enzyme | Fusarium oxysporum | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.45 | 9 | - |
assay at | Fusarium oxysporum |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.45 | evolution | the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX | Fusarium oxysporum |
| 1.13.11.45 | additional information | structure-function analysis | Colletotrichum gloeosporioides |
| 1.13.11.45 | additional information | structure-function analysis | Fusarium oxysporum |
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