Abstract
Glutamate dehydrogenase (E.C.1.4.1.3), or GDH, from beef liver is relatively nonspecific towards both its amino acid substrate (1, 2) and its pyridine nucleotide coenzyme (3, 4, 5). However, the unusual opportunity this offers for testing the mechanism by detailed comparative kinetic studies has been neglected. After Olson and Anfinsen discovered activation of glutamate oxidation by high levels of NAD (3), later workers concentrated on the supposedly simpler reaction with NADP. Although GDH has been cited (6) as an example of an allosteric enzyme, reliable, detailed kinetic data to support this suggestion have been lacking till now.
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Engel, P.C., Dalziel, K. (1970). Kinetics and Mechanism of Glutamate Dehydrogenase. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_22
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DOI: https://doi.org/10.1007/978-3-642-49974-6_22
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