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Am J Physiol Regul Integr Comp Physiol 237: R167-R173, 1979;
0363-6119/79 $5.00
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AJP - Regulatory, Integrative and Comparative Physiology, Vol 237, Issue 3 167-R173, Copyright © 1979 by American Physiological Society

ARTICLES

Computer simulation of metabolism in pyruvate-perfused rat heart. III. Pyruvate dehydrogenase

M. C. Kohn, M. J. Achs and D. Garfinkel

A physiologically and biochemically realistic model of the regulation of pyruvate dehydrogenase complex (PDH) was constructed for the perfused rat heart. It includes conversion between inactive (phospho) and active (dephospho) forms by a specific protein kinase (PDHK) and phosphoprotein phosphatase (PDHP). The activity of the tightly bound PDHK is influenced by synergistic activation/inhibition by acetyl CoA/CoASH and NADH/NAD. PDHK in this simulation was more sensitive to the fraction of ADP that was Mg2+-chelated than to the ATP-to-ADP ratio. Ca2+ stimulates binding of Mg2+-dependent PDHP to the complex; the bound enzyme was considered to be the active species. The fraction of PDH in the active form, rather than substrate and inhibitor levels, determines PDH activity under these conditions. This fraction depends on the present value and recent history of the difference between PDHK and PDHP activities. Both of these are active continuously and continuously control PDH.


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N. H. Jeoung and R. A. Harris
Pyruvate dehydrogenase kinase-4 deficiency lowers blood glucose and improves glucose tolerance in diet-induced obese mice
Am J Physiol Endocrinol Metab, July 1, 2008; 295(1): E46 - E54.
[Abstract] [Full Text] [PDF]


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