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Plant and Cell Physiology, 1977, Vol. 18, No. 5 963-968
© 1977

Article

Use of inhibitors to distinguish between C4 acid decarboxylation mechanisms in bundle sheath cells of C4 plants

C. K. M. Rathnam1 and G. E. Edwards

Department of Horticulture, University of Wisconsin Madison, Wisconsin-53706, U. S. A.

Both malate and aspartate were decarboxylated at the 4-carbon position by isolated bundle sheath strands of C4 plants but to different extents depending upon the species. In Digitaria sanguinalis, an NADP-malic enzyme (NADP-ME) species, 100 µM oxalic acid blocked malate decarboxylation through NADP-ME without affecting aspartate decarboxylation which apparently occurs through NAD-ME. In several phosphoenolpyruvate carboxykinase (PEP-CK) type C4 species, 200 µM 3-mercaptopicolinic acid (3-MPA), an inhibitor of PEP-CK, specifically inhibited the malate decarboxylation and partially inhibited aspartate decarboxylation. The aspartate decarboxylation insensitive to 3-MPA may occur through NAD-ME. Neither inhibitor prevented C4 acid decarboxylation in bundle sheath cells of NAD-ME species. The inhibitors thus served to differentiate between the decarboxylation of C4 acids in PEP-CK and NADP-ME type C4 species through their major decarboxylase from that of their less active decarboxylation through NAD-ME.

1 Present address: Department of Biochemistry and Microbiology, Rutgers University, New Brunswick, NJ 08903, U. S. A.

(Received January 28, 1977; )
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