FEBS Letters | |
All three acyl moieties of trilinolein are efficiently oxygenated by recombinant His‐tagged lipid body lipoxygenase in vitro | |
Kindl, Helmut2  Höhne, Michaela2  Bachmann, Astrid1  Feussner, Ivo1  | |
[1] Institut für Pflanzenbiochemie, Weinberg 3, D-06120 Halle, Germany;Fachbereich Chemie, Philipps-Universität, Hans-Meerwein-Str., D-35032 Marburg, Germany | |
关键词: Cucumber; Oxygenation of trilinolein; Soybean lipoxygenase; Substrate specificity; | |
DOI : 10.1016/S0014-5793(98)00808-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Recently, we found a 13-lipoxygenase in germinating cucumber cotyledons, which was located at the lipid body membrane. Based on its products formed mobilization of storage lipids seems to be initiated by this 13-lipoxygenase. For biochemical characterization its cDNA was expressed as His-tagged protein. Active recombinant enzyme was obtained from low temperature cultivation of E. coli after affinity purification. It (i) exhibited an unchanged region specificity, and (ii) showed a pH optimum of 7.2 against trilinolein as substrate. We compared its ability to oxygenate trilinolein with the one of another 13-lipoxygenase, soybean lipoxygenase-1. At the pH optimum of soybean lipoxygenase-1 (9.0), trilinolein was oxygenated only to 28% of the amount converted by the lipid body lipoxygenase. Moreover, trilinolein oxygenation by soybean lipoxygenase-1 leads mainly to monohydroperoxy derivatives, whereas oxygenation by lipid body LOX leads to a trihydroperoxy derivative.
【 授权许可】
Unknown
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