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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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Related references

Fahien, L.A.; Kmiotek, E., 1981: Regulation of glutamate dehydrogenase by palmitoyl-coenzyme A. Archives of Biochemistry and Biophysics 212(1): 247-253

Kawaguchi, A.; Bloch, K., 1976: Inhibition of glutamate dehydrogenase and malate dehydrogenases by palmitoyl coenzyme A. In extension of a previous study with yeast glucose-6-P dehydrogenase (Kawaguchi, A., and Bloch, K. (1974) J. Biol. Chem. 249, 5793-5800), the structural changes accompanying the inhibition of glutamate dehydrogenase and several malate dehydrogena...

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Ciardelli T.; Stewart C.J.; Seeliger A.; Wieland T., 1981: Synthesis of a carba analog of s palmitoyl coenzyme a heptadecan 2 onyl dethio coenzyme a and of s heptadecyl coenzyme a effective inhibitors of citrate synthase and carnitine palmitoyl transferase. The syntheses of two long chain alkyl-CoA derivatives and are reported. Heptadecan-2-onyldethio-CoA (1), a carba analog of S-palmitoyl-CoA, is obtained along with its 2'-phosphate isomer (11) by the condensation of adenosine 2',3'-c...

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Berge, R.K.; Vollset, S.E.; Farstad, M., 1980: Intra cellular localization of palmitoyl coenzyme a hydrolase ec 3.1.2.2 and palmitoyl coenzyme a synthetase ec 6.2.1.3 in human blood platelets and liver. The intracellular localization studies of human blood platelets by sucrose gradient and differential centrifugation showed that palmitoyl-CoA hydrolase was mainly localized in the cytosol fraction. A localization also in the mitochondrial fraction...

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