Activity oscillations predicted for pyruvate dehydrogenase complexes

Selivanov, Vitaly A.; Zakrzhevskaya, D.T.; Goldstein, B.N.

doi:10.1016/0014-5793(94)00425-0

Cited by 6 publications

(20 citation statements)

References 15 publications

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“…Moreover, these kinetic ;themes can describe the very steep change in metabolic fluxes ~nder the relatively low chemical regulatory signal, acting ',hrough El phosphorylation, for example. We have predicted '.he bistability effect [16] and oscillations in the fluxes [17]. Such nusual kinetic behavior was observed recently for some of the 1 aultienzyme complexes [18,19].…”

Section: Resultssupporting

confidence: 71%

“…This scheme allows us to write the 1, inetic equations, describing the kinetic behavior of the mull enzyme complex, Kinetic scheme in Fig. 2 is similar in its topological structure I) the kinetic schemes considered in our earlier works [16,17] ~tnd applied to the multienzyme complexes of the family under tiscussion. Now, the kinetic scheme for the mammalian pyavate dehydrogenase complex obtains its interpretation on the ,~elf-assembly model.…”

Section: Resultsmentioning

confidence: 99%

“…Now, the kinetic scheme for the mammalian pyavate dehydrogenase complex obtains its interpretation on the ,~elf-assembly model. The kinetic schemes of such a specific ~, lructure have been shown [16,17] to generate the kinetic behavi)r of a critical kind at certain parameter values due to the t ompetition of two kinetically different interconnected reaction lathways for the same substrate. Moreover, these kinetic ;themes can describe the very steep change in metabolic fluxes ~nder the relatively low chemical regulatory signal, acting ',hrough El phosphorylation, for example.…”

Section: Resultsmentioning

confidence: 99%

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Principles of symmetrical organization for the pyruvate dehydrogenase complex

1995

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The experimentally observed phenomenon of nonequimolarity for enzyme compoeents, assembled into mnltien7yme complexes of the 2-oxo acid dehydrogenases family, is structurally interpreted to predict the only possible stable symmetrical distribution of peripheral components on the complex core. To obey the equivalent neighboring, that is necessary for unique self-assembled structures, we should deduce discrete conformational states for core subunlts, those with different affinity for peripheral components. Two kinetically different types of substrate-intermediate pathways through the lipoyl network of the mammalian pyruvate dehydrogenase complex follow from this structural theory. The theory predicts unusual kinetic behavior for the multienzyme complex.

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Section: Resultssupporting

confidence: 71%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Principles of symmetrical organization for the pyruvate dehydrogenase complex

1995

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“…It turned out that not only well‐known substrate inhibition and product activation induce oscillations. Any competition of a single, channeled intermediate for multiple active sites in multienzyme complexes can also induce oscillatory kinetics [28].…”

Section: Discussionmentioning

confidence: 99%

“…Two negative paths in the cycle of subgraphs here reflect the competition of two reactions for a single species. For example, the competition of protein X and the enzyme E 2 for the acetyl group in pyruvate dehydrogenase complex has been shown to be important for the prediction of oscillatory behavior [28].…”

Section: Examples Of Biochemical Oscillationsmentioning

confidence: 99%

What makes biochemical networks tick?

Goldstein

Ermakov

Centelles

et al. 2004

European Journal of Biochemistry

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In view of the increasing number of reported concentration oscillations in living cells, methods are needed that can identify the causes of these oscillations. These causes always derive from the influences that concentrations have on reaction rates. The influences reach over many molecular reaction steps and are defined by the detailed molecular topology of the network. So-called Ôautoinfluence pathsÕ, which quantify the influence of one molecular species upon itself through a particular path through the network, can have positive or negative values. The former bring a tendency towards instability. In this molecular context a new graphical approach is presented that enables the classification of network topologies into oscillophoretic and nonoscillophoretic, i.e. into ones that can and ones that cannot induce concentration oscillations. The network topologies are formulated in terms of a set of uni-molecular and bi-molecular reactions, organized into branched cycles of directed reactions, and presented as graphs. Subgraphs of the network topologies are then classified as negative ones (which can) and positive ones (which cannot) give rise to oscillations. A subgraph is oscillophoretic (negative) when it contains more positive than negative autoinfluence paths. Whether the former generates oscillations depends on the values of the other subgraphs, which again depend on the kinetic parameters. An example shows how this can be established. By following the rules of our new approach, various oscillatory kinetic models can be constructed and analyzed, starting from the classified simplest topologies and then working towards desirable complications. Realistic biochemical examples are analyzed with the new method, illustrating two new main classes of oscillophore topologies.

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Switching mechanism for branched biochemical fluxes: Graph-theoretical analysis

Goldstein

2007

Biophysical Chemistry

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Activity oscillations predicted for pyruvate dehydrogenase complexes

Cited by 6 publications

References 15 publications

Principles of symmetrical organization for the pyruvate dehydrogenase complex

Principles of symmetrical organization for the pyruvate dehydrogenase complex

What makes biochemical networks tick?

Switching mechanism for branched biochemical fluxes: Graph-theoretical analysis

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