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Literature summary for 1.13.11.B6 extracted from

  • Cho, K.; Jang, S.; Huon, T.; Park, S.; Han, O.
    Biochemical characterization of the dual positional specific maize lipoxygenase and the dependence of lagging and initial burst phenomenon on pH, substrate, and detergent during pre-steady state kinetics (2007), J. Biochem. Mol. Biol., 40, 100-106.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
beta-cyclodextrin
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Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
linoleate + O2 the dual positional specific maize lipoxygenase is not able to catalyze the oxidation of trilinolein or trilinolenin even in the presence of detergent. The enzyme seems to ultilize only free fatty acid as a substrate. The solubilization of substrate involves the incorporation of substrate molecules into the detergent micelles, which leads to decreased availability of effective free fatty acids for binding with the LOX enzyme. The unique initial burst phenomenon of the maize LOX observed in the oxidation of linoleate at low pH may also be attributed to the availability of free fatty acids as substrates Zea mays (10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E)-13-hydroperoxy-9,11-octadecadienoate
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