Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 81:115-119 (1986)
© 1986 American Society of Plant Biologists

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Articles

The Involvement of Aspartate and Glutamate in the Decarboxylation of Malate by Isolated Bundle Sheath Chloroplasts from Zea mays

Stuart Boag and Colin L. D. Jenkins

CSIRO, Division of Plant Industry, GPO Box 1600, Canberra A.C.T. 2601, Australia

Aspartate or glutamate stimulated the rate of light-dependent malate decarboxylation by isolated Zea mays bundle sheath chloroplasts. Stimulation involved a decrease in the apparent Km (malate) and an increased maximum velocity of decarboxylation. In the presence of glutamate other dicarboxylates (succinate, fumarate) competitively inhibited malate decarboxylation by intact chloroplasts with respect to malate with an apparent Ki of about 6 millimolar. For comparison the Ki for inhibition of nicotinamide adenine dinucleotide phosphate-malic enzyme from freshly lysed chloroplasts by these dicarboxylates was 15 millimolar. A range of compounds structurally related to aspartate stimulated malate decarboxylation by intact chloroplasts. Ka values for stimulation at 5 millimolar malate were 1.7, 5, and 10 millimolar for L-glutamate, L-aspartate, and {beta}-methyl-DL-aspartate, respectively. Certain compounds, notably cysteic acid, which stimulated malate decarboxylation by intact chloroplasts inhibited malate decarboxylation by nicotinamide adenine dinucleotide phosphate-malic enzyme obtained from lysed chloroplasts and assayed under comparable conditions. It was concluded that aspartate, glutamate, and related compounds affect the transport of malate into the intact chloroplasts and that malate translocation does not take place on the general dicarboxylate translocator previously reported for higher plant chloroplasts.




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Copyright © 1986 by the American Society of Plant Biologists