| Abstract: | Characteristics of glycolate-oxidizing enzymes in crude extracts of algal species in the Chlorophyta, Chromophyta, Prymnesiophyta, Dinophyta, Cryptophyta, and Rhodophyta were compared by measuring glycolate-dependent O2 consumption and dichlorophenolindophenol (DCPIP) reduction under anaerobic conditions and by checking cyanide sensitivity and the stereospecificity for d - and l -lactate. Glycolate dehydrogenase similar to that found in the Chlorophyceae was found only in the Prasinophyceae, which is phylogenetically close to the Chlorophyceae, and in the Cryptophyta, the phylogenetically enigmatic algae. Glycolate oxidase was found in the Chromophyta except the Bacillariophyceae and in the rhodophyte Porphyridium purpureum (Bory) Drew & Ross. No detectable activity was found in the other rhodophytes, dinoflagellates, or prymnesiophytes. Glycolate dehydrogenase in the Bacillariophyceae was not cyanide-sensitive and had a stereospecificity for l -lactate. Catalase activity was observed at high levels in all algae possessing glycolate oxidase, but was not detected in the Bacillariophyceae, Prasinophyceae, and Cryptophyta, which have glycolate dehydrogenase activity. High levels of d -lactate-dependent DCPIP-reducing activity were observed in the raphidophyte Heterosigma akashiwo (Hada) Hada, a major constituent of red tides on the coast of Japan, and in the Bacillariophyceae, but such activity was not catalyzed by the glycolate-oxidizing enzymes nor NAD-dependent lactate-oxidizing enzymes. |
