%0 Journal Article %A Kumar, Sharad %A Nicholas, D. J. D. %T NAD+ - and NADP+-Dependent Glutamate Dehydrogenases in Nitrobacter agilis %D 1984 %J Microbiology, %V 130 %N 4 %P 967-973 %@ 1465-2080 %R https://doi.org/10.1099/00221287-130-4-967 %I Microbiology Society, %X Two isoenzymes of glutamate dehydrogenase located in the cytoplasmic fraction of Nitrobacter agilis were specific for NAD+ and NADP+, respectively. The NAD+-dependent enzyme functioned in both directions, i.e. amination and deamination, whereas the NADP+ enzyme was primarily for the amination of 2-oxoglutarate to glutamate. The NADP+ enzyme was purified 52-fold (free of the NAD+ enzyme) by affinity chromatography on 2′,5′-ADP Sepharose 4B, and some of its properties studied. Substrate activation of the amination reaction of the NADP+ enzyme was observed with NH+ 4 and NADPH. A comparison is made of the properties of the purified NADP+ enzyme from Nitrobacter agilis and Nitrosomonas europaea. The possible roles of two isoenzymes of glutamate dehydrogenase in Nitrobacter agilis are discussed. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-130-4-967