
%0 Journal Article
%A Chapman, KSR 
%A Hatch, MD 
%T Aspartate Decarboxylation in Bundle Sheath Cells of <I>Zea mays</I> and Its Possible Contribution to C<sub>3</sub> Photosynthesis
%J Functional Plant Biology
%D 1981/04/01
%V 8
%N 2
%P 237-248
%K 
%R https://doi.org/10.1071/PP9810237
%U https://www.publish.csiro.au/paper/PP9810237 
%X Strands of bundle sheath cells isolated from the NADP malic enzyme type C4 species, Zea mays, rapidly decarboxylate malate via NADP malic enzyme. The present studies show that these cells also decarboxylate aspartate, but at much lower rates. Aspartate decarboxylation is dependent upon added 2-oxoglutarate, is partially light dependent, and apparently proceeds via the following reaction sequence: aspartate &#859;4 oxaloacetate &#859;4 malate &#859;4 pyruvate + CO2. Studies of the activity, properties, and location of enzymes indicated that these reactions are catalysed by a mitochondrial aspartate aminotransferase, mitochondrial or cytoplasmic NAD malate dehydrogenase, and chloroplast-located NADP malic enzyme, respectively. A mitochondria preparation isolated from Z. mays bundle sheath cells converted aspartate to oxaloacetate (with 2-oxoglutarate) and also pyruvate to alanine (with glutamate); the preparation did not reduce oxaloacetate to malate or decarboxylate malate at significant rates.    Bundle sheath strands of Z. mays have a relatively limited capacity for HCO3- plus ribose 5-phosphate dependent oxygen evolution and rates were almost as high with aspartate plus 2-oxoglutarate. We suggest that amongst NADP malic enzyme type C4 species there may be a direct relationsip between the capacity of bundle sheath cells to decarboxylate aspartate and their potential for the photosystem II-mediated oxygen evolution. 
