Biosynthesis of Dicarboxylic Acids by Carbon Dioxide Fixation

pH dependence of the kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme

“…The second classification is EC 1.1.1.39 [l-malateiNAD oxidoreductase (decarboxylating)] which includes malic enzyme from the group D streptococcus (London & Meyer, 1969), cauliflower (MacRae, 1971), potato tuber (Grover et al, 1981), and Ascaris suum (Saz & Hubbard, 1957;Podge et al, 1972). Finally, the third type is EC 1.1.1.38 [L-malate:NAD oxidoreductase (oxalacetate-decarboxylating)] which includes malic enzyme from Lactobacillus arabinosus (Korkes et al, 1950) and the enzyme from the dung beetle Catharsius (Imbuga & Pearson, 1982). The class EC 1.1.1.38 exists only at low levels in vertebrates (Sauer, 1973a,b;Lin & Davis, 1974), but more activity is found in certain invertebrate tissues.…”

Potentiometric determination of nicotinamide adenine dinucleotide phosphate and glutathione reductase

“…The use of 0.8 M sodium phosphate buffer of the same pHs instead of potassium phosphate gives only 85-90% of the rate values. Potassium phosphate buffer of pH 6 recommended by other workers (26,32) for the reaction was used throughout this investigation.…”

Yield of oxidative phosphorylation associated with the oxidation of succinate to fumarate

“…Fumarate plus malate. The amount of (fumarate plus malate) present after oxidation of succinate by mitochondria or sarcosomes was determined by means of malic decarboxylase (Korkes, del Campillo & Ochoa, 1950;Nossal, 1951Nossal, , 1952. In these experiments, oxidation of succinate was carried out according to the procedure and with the same reaction mixture as described above for measurements of the P: 0 ratio, except that two concentrations of suceinate (6-6 mm and 66 mM) were used and the reaction volume was 1-5 ml.…”