OCCURRENCE OF GLYCOLATE OXIDASE AND HYDROXYPYRUVATE REDUCTASE IN EGREGIA MENZIESII (PHAEOPHYTA)1

Authors

  • Wolfgang Gross

    1. Biology Department. University of California at Santa Cruz, Santa Cruz. California 95064
    Search for more papers by this author
    • 2

      Department of Botany, North Carolina State University, Releigh, North Carolina 27695-7612.


  • 1

    Received 23 October 1989 Accepted 5 January 1990.

  • This work was supported by National Science Foundation (Grant PCM 84-03542) to Dr. H. Beevers and a postdoctoral fellowship (Feodor-Lyned Program) from the Alexander-von-Humboldt foundation (West Germany) to W.G.

ABSTRACT

Glycolate oxidase and hydroxypyruvate reductase, two key enzymes of glycolate metabolism, are present in the brown alga Egregia menziesii (Turn.) Aresch. The pH optimum and Km for the partially purified glycolate oxidase are similar to the enzyme from higher plants, Charophyta and Xanthophyta, whereas the substrate specificity is different from the higher plant enzyme.

Ancillary