Abstract
The complex behaviour of beef liver glutamate dehydrogenase towards a variety of effectors has been studied by a number of workers and particularly by Frieden (1) and Tomkins and his collaborators (2). While the metabolic significance (if any) of the inhibition by GTP and activation by ADP is not clear, the regulation of enzyme activity by small effector molecules is of general importance (3). Mechanistically the fundamental problem is one of energy transmission, as the free energy of interaction between a specific region of the enzyme and the effector will have to be relayed to the catalytic site. There, the energy could be utilized in distorting the favourable stereochemical arrangement of functionally important protein side-chains resulting in an adjustment of the kinetic or binding behaviour of the enzyme.
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Brocklehurst, J.R., Dodd, G.H., Freedman, R.B., Malcolm, A.D.B., Price, N.C., Radda, G.K. (1970). Optical Probes for Glutamate Dehydrogenase. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_23
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DOI: https://doi.org/10.1007/978-3-642-49974-6_23
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