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Regulation of glutamate dehydrogenase ec 1.4.1.3 by palmitoyl coenzyme a


, : Regulation of glutamate dehydrogenase ec 1.4.1.3 by palmitoyl coenzyme a. Archives of Biochemistry and Biophysics 212(1): 247-253

Glutamate dehydrogenase [bovine liver mitochondrin] is inhibited more by palmitoyl-CoA when TPNH instead of DPNH is the coenzyme. Inhibition is further enhanced by .alpha.-ketoglutarate and malate. Thus, for example, in the presence of TPNH plus malate, the amount of palmitoyl-CoA required for 50% inhibition is 10-fold lower (0.03 .mu.M) than previously reported values obtained with DPNH as a coenzyme. Allosteric modifiers such as ATP, GTP and leucine decrease inhibition of glutamate dehydrogenase by palmitoyl-CoA. Palmitoyl-CoA and ADP are competitive. Thus, the palmitoyl-CoA binding site is apparently in the vicinity of the site of these allosteric modifiers and is probably at the ADP site. The fact that ADP (which has only 1 site/polypeptide chain) can completely prevent inhibition by palmitoyl-CoA suggests that there is only 1 kinetically significant palmitoyl-CoA binding site per polypeptide chain. This is consistent with the fact that adding 1 equivalent of palmitoyl-CoA per polypeptide chain inhibits about 80%. The high affinity of glutamate dehydrogenase for palmitoyl-CoA enables it to successfully compete with other mitochondrial proteins for palmitoyl-CoA.

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