EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.11.12 | recombinant overexpression of His-tagged enzyme in Escherichia coli BL21(DE3) | Pseudomonas aeruginosa |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.13.11.12 | extracellular | the enzyme is secreted | Pseudomonas aeruginosa | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.12 | arachidonic acid + O2 | Pseudomonas aeruginosa | - |
(5Z,8Z,11Z, 13E,15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid | - |
? | |
1.13.11.12 | linoleic acid + O2 | Pseudomonas aeruginosa | - |
(9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate | - |
? | |
1.13.11.12 | 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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.12 | Pseudomonas aeruginosa | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.11.12 | recombinant His-tagged enzyme from Escherichia coli BL21(DE3)by nickel affinity chromatography and | Pseudomonas aeruginosa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.12 | arachidonic acid + O2 | - |
Pseudomonas aeruginosa | (5Z,8Z,11Z, 13E,15S)-15-hydroperoxy-5,8,11,13-eicosatetraenoic acid | - |
? | |
1.13.11.12 | linoleic acid + O2 | - |
Pseudomonas aeruginosa | (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate | - |
? | |
1.13.11.12 | 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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.12 | LOX | - |
Pseudomonas aeruginosa |
1.13.11.12 | PA-LOX | - |
Pseudomonas aeruginosa |
1.13.11.12 | secreted lipoxygenase | - |
Pseudomonas aeruginosa |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.12 | additional information | - |
additional information | kcat of the enzyme with mitochondrial membranes as substrate is 0.3/s | Pseudomonas aeruginosa | |
1.13.11.12 | 162.4 | - |
linoleic acid | pH and temperature not specified in the publication | Pseudomonas aeruginosa |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.12 | 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 |