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Articles

The Occurrence of Glycolate Dehydrogenase and Glycolate Oxidase in Green Plants

An Evolutionary Survey ¹

^a Department of Biochemistry, Michigan State University, East Lansing, Michigan 48823

Homogenates of various lower land plants, aquatic angiosperms, and green algae were assayed for glycolate oxidase, a peroxisomal enzyme present in green leaves of higher plants, and for glycolate dehydrogenase, a functionally analogous enzyme characteristic of certain green algae. Green tissues of all lower land plants examined (including mosses, liverworts, ferns, and fern allies), as well as three freshwater aquatic angiosperms, contained an enzyme resembling glycolate oxidase, in that it oxidized L- but not D-lactate in addition to glycolate, and was insensitive to 2 mM cyanide. Many of the green algae (including Chlorella vulgaris, previously claimed to have glycolate oxidase) contained an enzyme resembling glycolate dehydrogenase, in that it oxidized D- but not L-lactate, and was inhibited by 2 mM cyanide. Other green algae had activity characteristic of glycolate oxidase and, accordingly, showed a substantial glycolate-dependent O₂ uptake. It is pointed out that this distribution pattern of glycolate oxidase and glycolate dehydrogenase among the green plants may have phylogenetic significance.

Activities of catalase, a marker enzyme for peroxisomes, were also determined and were generally lower in the algae than in the land plants or aquatic angiosperms. Among the algae, however, there were no consistent correlations between levels of catalase and the type of enzyme which oxidized glycolate.

¹ This research was supported in part by National Science Foundation Grant GB-32040X and by a National Science Foundation Postdoctoral Fellowship to P. J.G. It is published as Journal Article No. 6357 of the Michigan Agricultural Experimental Station.

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