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Literature summary for 1.13.11.12 extracted from

  • Feussner, I.; Bachmann, A.; H๖hne, M.; Kindl, H.
    All three acyl moieties of trilinolein are efficiently oxygenated by recombinant His-tagged lipid body lipoxygenase in vitro (1998), FEBS Lett., 431, 433-436.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Cucumis sativus

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information lipid body Cucumis sativus
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Organism

Organism UniProt Comment Textmining
Cucumis sativus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
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Cucumis sativus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
linoleate + O2
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Cucumis sativus (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate the ratio of (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate is 87:13 for the enzyme from cucumber cotyledons, and 84:16 for the recombinant enzyme. A linoleate 9-LOX preferentially oxygenates free fatty acids whereas a linoleate 13-LOX is capable of oxygenating triolein to significantly higher degrees in all positions of the triacylglycerol. For 9-LOXs, the carboxylate anion of the substrate may be the binding or recognition site within the catalytic pocket of the enzyme, whereas in the case of 13-LOXs the unpolar hydrophobic tail of the fatty acid may be orientated towards the catalytic pocket of the enzyme. This may explain why unpolar substrates, such as trilinolein, are preferred substrates for linoleate 13-LOXs ?
additional information oxygenation of triolein by lipid body LOX leads to a trihydroperoxy derivative Cucumis sativus ?
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?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
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triolein as substrate Cucumis sativus

pH Range

pH Minimum pH Maximum Comment Organism
5.6 8.5 pH 5.6. about 50% of maximal activity, pH 8.5: about 70% of maximal activity Cucumis sativus