Abstract
Three enzymes assumed to mediate CO(2) metabolism in corn root tips, P-enolpyruvate carboxylase, malic dehydrogenase, and the malic enzyme, were extracted to determine their relative specific activities and their partitioning between soluble and particulate fractions. The data indicated that the intracellular location of these 3 enzymes is nonparticulate and thus these enzymatic reactions of CO(2) metabolism are apparently nonparticulate. The soluble malic dehydrogenase fraction differed from the particulate fraction in several kinetic properties, viz., response to the thionicotinamide analog of nicotinamide-adenine dinucleotide, oxaloacetate substrate inhibition at pH 8.3, and Km's for nicotinamide-adenine dinucleotide and l-malate. It was concluded that the soluble-malic dehydrogenase differed from the particulate forms in both structure and function. The soluble malic dehydrogenase is apparently involved in CO(2) metabolism.