Pyridine nucleotide independent oxidation of L-malate in genus Neisseria.
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.
D002474:Cell-Free System; D002952:Citric Acid Cycle; D008291:Malate Dehydrogenase / Q000378:metabolism*; D008293:Malates / Q000378:metabolism*; D009343:Neisseria / Q000201:enzymology / Q000378:metabolism*; D009344:Neisseria gonorrhoeae / Q000378:metabolism; D009345:Neisseria meningitidis / Q000378:metabolism; D010071:Oxaloacetates / Q000378:metabolism; D010084:Oxidation-Reduction; D011725:Pyridines / Q000378:metabolism*
D008293:Malates; D010071:Oxaloacetates; D011725:Pyridines; D008291:Malate Dehydrogenase