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Localization of β-oxidation enzymes in peroxisomes isolated from nonfatty plant tissues

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Abstract

Peroxisomes from spinach leaves, mungbean hypocotyls, and potato tubers catalyze a palmitoyl-CoA-dependent, KCN-insensitive O2 uptake. In the course of this reaction O2 is reduced to H2O2 in a 1:1 stoichiometry and palmitoyl-CoA oxidized, in a 1:1 stoichiometry, to a product serving as substrate for enoyl-CoA hydratase. These findings demonstrate the existence of a peroxisomal acyl-CoA oxidase in these tissues. Enoyl-CoA hydratase (EC 4.2.1.17), 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35), and thiolase (EC 2.3.1.9) are also associated with the peroxisomes from mung-bean hypocotyls and potato tubers (as well as with spinach leaf peroxisomes as recently reported; Gerhardt 1981, FEBS Lett. 126, 71). The low activities of these enzymes in mitochondrial fractions seem to be due to contaminating peroxisomes since the ratio of β-oxidation enzyme activities to catalase activity did not significantly differ between peroxisomal and mitochondrial fractions isolated on sucrose density gradients. The proof of localization of β-oxidation enzymes in peroxisomes without glyoxysomal function leads to the concept that fatty-acid oxidation is a consistent basic function of the peroxisome in cells of higher plants.

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Abbreviations

HDH:

3-hydroxyacyl-CoA dehydrogenase

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  1. Botanisches Institut der Universität, Schlossgarten 3, D-4400, Münster, Federal Republic of Germany

    B. Gerhardt

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  1. B. Gerhardt
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Dedicated to Professor Martin Bopp on occasion of his 60th birthday

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Gerhardt, B. Localization of β-oxidation enzymes in peroxisomes isolated from nonfatty plant tissues. Planta 159, 238–246 (1983). https://doi.org/10.1007/BF00397531

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  • DOI: https://doi.org/10.1007/BF00397531

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