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Literature summary for 1.13.11.12 extracted from
- Secreted lipoxygenase from Pseudomonas aeruginosa exhibits biomembrane oxygenase activity and induces hemolysis in human red blood cells (2015), Arch. Biochem. Biophys., 584, 116-124 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant overexpression of His-tagged enzyme in Escherichia coli BL21(DE3) | Pseudomonas aeruginosa |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Pseudomonas aeruginosa | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arachidonic acid + O2 | Pseudomonas aeruginosa | - |
(5Z,8Z,11Z, 13E,15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid | - |
? |  |
| linoleic acid + O2 | Pseudomonas aeruginosa | - |
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate | - |
? | |
| additional information | Pseudomonas aeruginosa | mitochondrial membrane oxygenase activity of the enzyme PA-LOX, overview. PA-LOX is capable of oxygenating both, arachidonic acid and linoleic acid, the two major polyenoic fatty acids found in animal biomembranes. The enzyme binds phospholipids at its active site | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli BL21(DE3)by nickel affinity chromatography and | Pseudomonas aeruginosa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arachidonic acid + O2 | - |
Pseudomonas aeruginosa | (5Z,8Z,11Z, 13E,15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid | - |
? | |
| linoleic acid + O2 | - |
Pseudomonas aeruginosa | (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate | - |
? | |
| additional information | mitochondrial membrane oxygenase activity of the enzyme PA-LOX, overview. PA-LOX is capable of oxygenating both, arachidonic acid and linoleic acid, the two major polyenoic fatty acids found in animal biomembranes. The enzyme binds phospholipids at its active site | Pseudomonas aeruginosa | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| LOX | - |
Pseudomonas aeruginosa |
| PA-LOX | - |
Pseudomonas aeruginosa |
| secreted lipoxygenase | - |
Pseudomonas aeruginosa |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kcat of the enzyme with mitochondrial membranes as substrate is 0.3/s | Pseudomonas aeruginosa | |
| 162.4 | - |
linoleic acid | pH and temperature not specified in the publication | Pseudomonas aeruginosa | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | secreted lipoxygenase from Pseudomonas aeruginosa exhibits biomembrane oxygenase activity and induces hemolysis in human red blood cells. Secreted lipoxygenase oxygenates free arachidonic acid predominantly to 15S-hydro(peroxy)-5Z,8Z,11Z,13E-eicosatetraenoic acid. The enzyme is capable of binding phospholipids at its active site and physically interacts with model membranes | Pseudomonas aeruginosa |
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