Many wild-type strains of Neurospora crassa produce two glutamic dehydrogenases, one specific for triphosphopyridine nucleotide and another for diphosphopyridine nucleotide. The enzymes have been separated from one another and purified about 50-fold. Michaelis constants have been reported for various substrates. The pH optima of the DPN- and TPN-specific enzymes are 8.3 and 7.5 respectively.The possible reasons for the presence of two different enzymes catalyzing the same reaction are discussed.
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