Supramolecular organization of glycolytic enzymes

Bi, Kurganov; Sugrobova, N P; Mil'man, L S

doi:10.1016/s0022-5193(85)80086-2

Cited by 67 publications

(45 citation statements)

References 57 publications

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“…However, now it is becoming clear that microcompartments related to multi-enzyme complexes and metabolic channeling, as described above, are the principal basis of organization and compartmentation of cellular metabolism. They are formed by specific protein-protein interactions within multi-enzyme complexes that are due to macromolecular crowding, anchoring of glycolytic [40][41][42][43] and other enzymes to the cytoskeleton, or membrane channels and transporters [43][44][45][46][47][48]. Investigations carried out in Clegg and Deutscher's laboratories have shown that mammalian cells behave as highly organized macromolecular assemblies dependent on the cytoskeleton [47,48].…”

Section: Compartmentation Phenomenon and Vectorial Metabolismmentioning

confidence: 99%

“…Multi-enzyme complexes may be of different size and may even include whole metabolic pathways; these are then called metabolons, according to the terminology introduced by Paul Srere in 1985 [49]. Thus, there are glycolytic metabolons [41,45], Krebs cycle metabolons [50], and others [51,52]. New techniques such as FRET have been developed to study and visualize microcompartmentation, e.g., the study of microcompartmentation of cyclic AMP [53,54].…”

Section: Compartmentation Phenomenon and Vectorial Metabolismmentioning

confidence: 99%

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Integrated and Organized Cellular Energetic Systems: Theories of Cell Energetics, Compartmentation, and Metabolic Channeling

Saks

Monge

Anmann

et al. 2007

Molecular System Bioenergetics

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Bioenergetics as a part of biophysical chemistry and biophysics is a quantitative science that is based on several fundamental theories. The definition of energy itself is given by the first law of thermodynamics, and application of the second law of thermodynamics shows that living cells can function as open systems only where the internal order (low entropy state) is maintained due to increasing the entropy in the surrounding medium (Schrödinger's principle of negentropy). For this, the exchange of mass is needed, which gives rise to metabolism as the sum of catabolism and anabolism, and the free energy changes during catabolic reactions supply energy for all cellular work -osmotic, mechanical, and biochemical. The free energy changes during metabolic reactions obey the rules of chemical thermodynamics, which deals with Gibbs free energy of chemical reactions and with electrochemical potentials. For application of these theories to the integrated systems in vivo, complex cellular organization should be accounted for: macromolecular crowding; metabolic channeling and functional coupling mechanisms due to close and tight protein-protein interactions; compartmentation of the enzymes due to their attachment to the subcellular membranes or connection to the cytoskeleton; and both macro-and microcompartmentation of substrates and metabolites in the cells. Because of this, almost all processes important for cell life are localized within small areas of the cell, and for their integration effective systems of communication, including compartmentalized energy transfer systems, are required. These are represented in muscle cells by the phosphotransfer networks, mostly by the creatine kinase and adenylate kinase systems, whose alterations under ischemic conditions contribute significantly to acute ischemic contractile failure of the heart. 59 Molecular System Bioenergetics: Energy for Life. Edited by Valdur Saks

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Section: Compartmentation Phenomenon and Vectorial Metabolismmentioning

confidence: 99%

Section: Compartmentation Phenomenon and Vectorial Metabolismmentioning

confidence: 99%

Integrated and Organized Cellular Energetic Systems: Theories of Cell Energetics, Compartmentation, and Metabolic Channeling

Saks

Monge

Anmann

et al. 2007

Molecular System Bioenergetics

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“…Those studies were conducted at a stage when there was considerable interest in the concept that a myofibril-bound complex of glycolytic enzymes afforded an efficient means of regulating metabolic flux to meet the continually varying energy requirements of the muscle cell [49,50]. Much of the evidence purported to favor the concept of glycolytic enzyme adsorption to muscle thin filaments had been restricted to qualitative demonstrations of interactions at low ionic strength.…”

Section: Interaction Of Aldolase With the Myofibrillar Matrixmentioning

confidence: 99%

Determination of binding constants by affinity chromatography

Winzor

2004

Journal of Chromatography A

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“…This organization may be conceived either as a large 'static' multienzyme aggregate or as an equilibrium mixture of smaller, probably pairwise complexes existing in competitive equilibria. Mowbray and Moses [32] estimated the molecular mass for a complete glycolytic complex to be about 1.5 MDa, and Kurganov et al [33] gave a value of 2.6 MDa on the basis of a theoretical model. However, the existence of such a large complex is rather questionable: nothing of the kind has been observed in muscle and yeast cytosol [2].…”

Section: Genase and Yeast Aldolase -Phosphofructokinase Complexesmentioning

confidence: 99%

Interaction of enzymes involved in triosephosphate metabolism

Tompa¹,

Bär²,

Batke³

1986

European Journal of Biochemistry

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The affinity of baker's yeast (Saccharomyces cerevisiae) fructose-l,6-bisphosphate aldolase towards the metabolically related enzymes phosphofructokinase and glyceraldehyde-3-phosphate dehydrogenase was tested by using a fluorescence-probe technique with fluorescein isothiocyanate attached covalently to the enzymes. The dissociation constants of the enzyme-enzyme complexes, as well as the rate constants of association and dissociation, were determined. Data were compared with the parameters derived from a mammalian (rabbit muscle) system, known from the literature and determined under the same conditions (pH 7.5 or 8.5 in 0.05 M Tris/HCl buffer at 20°C). The comparison reveals similarities in the supramolecular organization of these cytoplasmic enzymes in phylogenetically distant species. Moreover, the fact that in vitro hybrid complexes are formed of stability comparable to that of non-hybrid complexes indicates that this ancient characteristic is probably conserved during evolution.A possible regulatory mechanism is presented, based on the dynamic competition, with each other, of the enzymes involved in triosephosphate metabolism.Recent isotope dilution experiments with reconstituted trienzyme complexes [l] (and Orosz, F. and Ovhdi, J., unpublished) showed the compaitmentation of triosephosphates to be a likely feature of mammalian muscle metabolism (cf. [l, 21). Physicochemical and kinetic studies on interactions of muscle enzymes located at the crossroad of triosephosphdte metabolic flow have also been performed [3-51 (and references in [6]). The majority of the available quantitative information (dissociation constants, rate constants of dissociation and association of these complexes) was obtained from fluorescence anisotropy measurements of the painvise interactions of fructose-l,6-bisphosphate aldolase and enzymes metabolically related to it. More recently efforts have also been made to characterize enzyme-enzyme interactions in cytoplasmic-like media prepared from the cell [2].

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Supramolecular organization of glycolytic enzymes

Cited by 67 publications

References 57 publications

Integrated and Organized Cellular Energetic Systems: Theories of Cell Energetics, Compartmentation, and Metabolic Channeling

Integrated and Organized Cellular Energetic Systems: Theories of Cell Energetics, Compartmentation, and Metabolic Channeling

Determination of binding constants by affinity chromatography

Interaction of enzymes involved in triosephosphate metabolism

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