Carbon Dioxide Fixation into Oxalacetate in Higher Plants.

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Abstract
Assay procedures have been described for detecting pepcarboxylase and pepcarboxykinase (pep: phosphoenol pyru-vate) in the tissues of higher plants, with special attention to the problems encountered in assay when the two enzymes are present in the same extract. Both enzymes were shown to be widely distributed in plant tissues. They frequently occur in the same source. The pepcarboxykinase of higher plants is specific for ATP rather than other nucleotides. Anomalous results with spinach particulates showed that oxalacetic acid formation from PEP was enhanced by ADP and IDP, though other tests for pepcarboxykinase were negative. The pepcarboxylase of spinach was localized in particulates. In cauliflower buds and pea seedlings, both the mitochondrial and the cytoplasmic proteins appeared to contain both enzymes, though in different amounts.