PMID: 1251Nov 15, 1975

The pyruvate-dehydrogenase complex from Azotobacter vinelandii. 2. Regulation of the activity

European Journal of Biochemistry
T W BrestersC Veeger


The presence of activators(AMP and sulphate) or inhibitors(acetyl-CoA) has no influence on the Hill coefficient of the S-shaped [pyruvate]--velocity curve of either the pyruvate-NAD+ overall reaction(h equals 2.5) or that of the pyruvate-K3Fe(CN)6 ACTIVITY OF THE FIRST ENZYME (H EQUALs 1.3). pH STUDIES INDICATED THAT THE Hill coefficient is dependent on subunit ionization within the pyruvate-containing complex and not on those in the free complex. It is concluded that pyruvate conversion rather that pyruvate binding is responsible for the allosteric pattern. The activity is due to absence of a protein kinase, mainly regulated at the acetyl-CoA/CoA, and NADH/NAD+ levels and by the value of the energy charge.


Nov 15, 1975·European Journal of Biochemistry·T W BrestersC Veeger
Aug 10, 1966·Biochimica Et Biophysica Acta·H G Hansen, U Henning
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Jun 1, 1983·Molecular and Biochemical Parasitology·R KomunieckiM Coulson
Jan 1, 1982·Annals of the New York Academy of Sciences·H J BosmaG Voordouw
Nov 15, 1975·European Journal of Biochemistry·T W BrestersC Veeger
Oct 16, 1999·European Journal of Biochemistry·A F HengeveldA de Kok
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