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PYRIDINE NUCLEOTIDE INDEPENDENT OXIDATION OF L‐MALATE IN GENUS NEISSERIA
Author(s) -
Holten Eirik
Publication year - 1976
Publication title -
acta pathologica microbiologica scandinavica section b microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-131X
DOI - 10.1111/j.1699-0463.1976.tb01895.x
Subject(s) - malate dehydrogenase , biochemistry , enzyme , electron acceptor , nucleotide , ferricyanide , nad+ kinase , chemistry , dehydrogenase , biology , gene
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.