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Plant Physiology 75:531-533 (1984)
© 1984 American Society of Plant Biologists

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Enzymes of {beta}-Oxidation in Different Types of Algal Microbodies

Helmut Stabenau1, U. Winkler and W. Säftel

Biology Department, University of California, Santa Cruz, California 95064, Universität Oldenburg, Fachbereich Biologie, Postfach 2503, D-2900 Oldenburg, West Germany

The algae Mougeotia and Eremosphaera were used for isolation of microbodies with the characteristics of leaf peroxisomes and unspecialized peroxisomes, respectively. In both types of organelles, the following enzymes of the {beta}-oxidation pathway were determined: acyl-CoA oxido-reductase, enoyl-CoA hydratase, and 3-hydroxyacyl-CoA dehydrogenase. There are indications that the peroxisomal oxidoreductase of both algae is a H2O2-forming oxidase rather than a dehydrogenase.

The enzymes enoyl-CoA hydratase and acyl-CoA oxidoreductase are located also in the mitochondria from Eremosphaera but not from Mougeotia. The mitochondrial acyl-CoA oxidizing enzyme was found to be a dehydrogenase. The specific activities of acyl-CoA oxidase and enoyl-CoA hydratase are lower than in spinach leaf peroxisomes. However, the activity of 3-hydroxyacyl-CoA dehydrogenase in the peroxisomes of both algae is almost 2-fold higher. The capability for degradation of fatty acids is a common feature of all different types of peroxisomes from algae.


1 Present address: Universität Oldenburg, Fachbereich Biologie, Postfach 2503, D-2900 Oldenburg, West Germany.




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U. Winkler, W. Saftel, and H. Stabenau
A New Type of a Multifunctional beta -Oxidation Enzyme in Euglena
Plant Physiology, February 1, 2003; 131(2): 753 - 762.
[Abstract] [Full Text] [PDF]




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Copyright © 1984 by the American Society of Plant Biologists