EC Number   |
Activating Compound |
Reference |
|---|
    1.13.11.33 | 12(S)-hydroperoxyeicosatetraenoic acid |
reduces the kinetic lag phase |
702324 |
| 1.13.11.33 | 13(S)-hydroperoxyoctadecadienoic acid |
activates 15-hLO-1 and removes the kinetic lag phase |
702324 |
| 1.13.11.33 | 13-(S)-hydroxyoctadecadienoic acid |
allosteric effector, which changes the conformation of 15-hLO-2 such that substrate affinity toward linoleic acid is significantly increased |
702344 |
| 1.13.11.33 | 13-hydroperoxy-octadecadienoic acid |
- |
706032 |
| 1.13.11.33 | 15(S)-hydroperoxyeicosatetraenoic acid |
activates 15-hLO-1 and removes the kinetic lag phase |
702324 |
| 1.13.11.33 | Acetylsalicylic acid |
ASA, 40% activation of 15(S)-HETE production at 0.02 mM in ASA-sensitive asthmatic patients |
686173 |
| 1.13.11.33 | mannitol |
osmotic activation of nasal tissue with mannitol activates 15-LO-1 leading to increased amounts of 15(S)-hydroxyeicosatetranoic acid in nasal lavage, and the levels of 15(S)-hydroxyeicosatetranoic acid are associated with nasal symptoms |
706579 |
| 1.13.11.33 | more |
15-LOX2 in NHP cells is positively regulated by Sp1, the enzyme is induced in cell senescence |
689842 |
| 1.13.11.33 | more |
ALOX15 is usually present as catalytically silent ferrous enzyme. To initiate fatty acid oxygenation, the enzyme must first be oxidized to a ferric form capable of initiating hydrogen abstraction. Unfortunately, single activation of the enzyme is not sufficient to keep it running, since during catalysis small quantities of radical intermediates might escape from the active site leaving the enzyme in an inactive ferrous (Fe2+) form. To keep the reaction at quasistationary levels, repeated enzyme activation is required and the primary oxygenation products appear to serve as enzyme activators. In this sense, the LOX exhibits autocatalytic properties |
742613 |
| 1.13.11.33 | more |
ALOX15 is usually present as catalytically silent ferrous enzyme. To initiate fatty acid oxygenation, the enzyme must first be oxidized to a ferric form capable of initiating hydrogen abstraction. Unfortunately, single activation of the enzyme is not sufficient to keep it running, since during catalysis small quantities of radical intermediates might escape from the active site leaving the enzyme in an inactive ferrous (Fe2+) form. To keep the reaction at quasistationary levels, repeated enzyme activation is required and the primary oxygenation products appear to serve as enzyme activators. In this sense, the LOX exhibits autocatalytic properties. Studying the oxygenation of 15S-HETE by pure rabbit ALOX15, it is found that the corresponding oxygenation product(s) does not activate the enzyme, while molecular dioxygen serves not only as a lipoxygenase substrate, but also impacts peroxide-dependent enzyme activation |
742613 |
