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Planta

, Volume 175, Issue 1, pp 91–98 | Cite as

β-Oxidation of fatty acids in algae: Localization of thiolase and acyl-CoA oxidizing enzymes in three different organisms

  • U. Winkler
  • W. Säftel
  • H. Stabenau
Article

Abstract

In the algae Mougeotia, Bumilleriopsis and Eremosphaera, recently shown to possess the enzymes hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) and enoyl-CoA hydratase (EC 4.2.1.17), the presence of thiolase (EC 2.3.1.9) and acyl-CoA-oxidizing enzymes can also be demonstrated, indicating that β-oxidation of fatty acids is possible in these organisms. The compartmentation of enzymes is different in the various algae. In Mougeotia, both thiolase and the acyl-CoA-oxidizing enzyme are located exclusively in the peroxisomes. The latter enzyme was found to be an oxidase using molecular oxygen as an electron acceptor. On the other hand, in Bumilleriopsis all enzymes of the fatty-acid β-oxidation pathway tested are constituents only of the mitochondria, and acyl-CoA is oxidized by a dehydrogenase incapable of reducing oxygen. Finally, in Eremosphaera thiolase and acyl-CoA-oxidizing enzymes were found in the peroxisomes as well as in the mitochondria. In the peroxisomes, oxidation of acyl-CoA is catalyzed by an oxidase, whereas the corresponding enzyme in the mitochondria is a dehydrogenase. The acyl-CoA oxidases/dehydrogenases of the three algae differ not only by their capability for oxidation of acyl-CoA of different chain lengths but also with regard to their Km values and substrate specificities. Indications were obtained that the oxygen is reduced to water rather than to H2O2 by the algal acyl-CoA oxidases. When cells of Eremosphaera were cultured with hypolipodemic substances in the growth medium the activities of the peroxisomal enzymes, but not those of the mitochondrial enzymes of the fatty-acid β-oxidation pathway, were increased by a factor of two to three.

Key words

Acyl-CoA oxidation Bumilleriopsis Eremosphaera Mougeotia β-Oxidation Thiolase 

Abbreviations

DPIP

2,6-dichlorophenol indophenol

INT

p-iodonitrotetrazolium violet

MEHP

monoethylhexylphthalate

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Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • U. Winkler
    • 1
  • W. Säftel
    • 1
  • H. Stabenau
    • 1
  1. 1.Fachbereich BiologieUniversität OldenburgOldenburgGermany

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