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  • Title: Pyridine nucleotide independent oxidation of L-malate in genus Neisseria.
    Author: Holten E.
    Journal: Acta Pathol Microbiol Scand B; 1976 Feb; 84(1):17-21. PubMed ID: 814782.
    Abstract:
    In cell free extract from Neisseria meningitidis an enzyme has been found which catalyses the oxidation of L-malate to oxaloacetate in the absence of pyridine nucleotides, using ferricyanide as electron acceptor. The enzyme was found to be particle-bound, as determined by sucrose gradient centrifugation. Activity corresponding to this enzyme was demonstrated in extracts from all strains tested of selected Neisseria species. In contrast to the large differences in NAD-linked malate dehydrogenase activity among the species, the interspecies variation of the pyridine nucleotide independent oxidation of malate was not sufficiently distinct to be useful for classification purposes.
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