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Literature summary extracted from

  • Mei, G.; Di Venere, A.; Nicolai, E.; Angelucci, C.B.; Ivanov, I.; Sabatucci, A.; Dainese, E.; Kuhn, H.; Maccarrone, M.
    Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability (2008), Biochemistry, 47, 9234-9242.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.33 BODIPY-D3825 competes with the substrate fatty acid for binding at the active site Glycine max
1.13.11.33 BODIPY-D3825 competes with the substrate fatty acid for binding at the active site Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.11.33 Ca2+ assay in presence of Ca2+ Oryctolagus cuniculus
1.13.11.33 Ca2+ assay in presence of Ca2+ Glycine max

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.33 Glycine max
-
-
-
1.13.11.33 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.33 by sequential ammonium sulfate precipitation, both cationic and anionic exchange chromatography and a fast protein liquid chromatography apparatus Glycine max
1.13.11.33 by sequential fractionated ammonium sulfate precipitation, hydrophobic interaction chromatography and anion exchange chromatography Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.13.11.33 reticulocyte
-
 Oryctolagus cuniculus
-
1.13.11.33 seed
-
 Glycine max
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.33 linoleic acid + O2
-
 Oryctolagus cuniculus (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
 ?
1.13.11.33 linoleic acid + O2
-
 Glycine max (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.33 12/15-lipoxygenase
-
 Oryctolagus cuniculus
1.13.11.33 12/15-LOX
-
 Oryctolagus cuniculus
1.13.11.33 15-LOX
-
 Glycine max

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.11.33 30
-
 structural alterations induced by increasing the temperature to 30°C are completely reversible, loss of reversibility at 35°C, aggregates between 45-50°C. The enzyme is thermolabile and requires the presence of a lipid environment to be stabilized at higher temperatures Oryctolagus cuniculus
1.13.11.33 45
-
 structural alterations induced by increasing the temperature to 45°C are completely reversible, loss of reversibility above 45°C, aggregates at 60°C. The enzyme is structurally stable and its membrane binding properties are hardly affected by temperature alterations Glycine max

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.13.11.33 0.001
-
 BODIPY-D3825
-
 Oryctolagus cuniculus
1.13.11.33 0.009
-
 BODIPY-D3825
-
 Glycine max

General Information

EC Number General Information Comment Organism
1.13.11.33 physiological function high degree of motional flexibility and a high membrane binding affinity Oryctolagus cuniculus
1.13.11.33 physiological function lower degree of motional flexibility in aqueous solutions than mammalian isozymes Glycine max