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Literature summary for 1.13.11.45 extracted from
- Expression and characterization of manganese lipoxygenase of the rice blast fungus reveals prominent sequential lipoxygenation of alpha-linolenic acid (2015), Arch. Biochem. Biophys., 583, 87-95 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene MGG_08499, DNA and amino acid sequence determination and analysis, recombinant expression and secretion of the enzyme in Pichia pastoris | Pyricularia oryzae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kineticss | Pyricularia oryzae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | enzyme-bound, is eliminated by denaturation of the enzyme protein | Pyricularia oryzae |  |
| Fe2+ | required, low amount bound to the enzyme | Pyricularia oryzae | |
| Mn2+ | required, high amount bound to the enzyme, exogenous Mn2+ does not enhance the enzyme activity | Pyricularia oryzae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyricularia oryzae | G4NAP4 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the deglycosylation process reduces the recombinant enzyme activity, but more than 50% is retained | Pyricularia oryzae |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant secreted enzyme 43fold from Pichia pastoris by hydrophobic interaction chromatography and gel filtration | Pyricularia oryzae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.01 | - |
purified recombinant enzyme, pH 9.0, 21°C | Pyricularia oryzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,2-dilinoleoyl-phosphatidylcholine + O2 | a poor substrate | Pyricularia oryzae | ? | - |
? | |
| 1-linoleoyl-2-hydroxy-phosphatidylcholine + O2 | an excellent substrate | Pyricularia oryzae | ? | - |
? | |
| linoleate + O2 | - |
Pyricularia oryzae | (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate | - |
? | |
| lyso-phosphatidylcholine + O2 | substrate from soybean | Pyricularia oryzae | ? | - |
? | |
| additional information | the enzyme can also convert linoleate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate, cf. linoleate 9S-lipoxygenase/EC 1.13.11.58 and linoleate 13R-lipoxygenase. Oxygen consumption monitoring | Pyricularia oryzae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 11000-130000, glycosylated recombinant enzyme, SDS-PAGE, x * 70000, about, deglycosylated recombinant enzyme, SDS-PAGE | Pyricularia oryzae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| manganese lipoxygenase | - |
Pyricularia oryzae |
| MGG_08499 | - |
Pyricularia oryzae |
| MnLOX | - |
Pyricularia oryzae |
| Mo-MnLOX | - |
Pyricularia oryzae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 21 | - |
assay at | Pyricularia oryzae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
the deglycosylation process slightly decreases the melting temperature of recombinant Mo-MnLOX from 60°C to 56°C | Pyricularia oryzae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
assay at | Pyricularia oryzae |
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Release 2023.1 (January 2023)
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