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Literature summary for 1.13.11.33 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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

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

Source Tissue

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

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
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]

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

General Information

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