Dissociation of mammalian D‐glyceraldehyde‐3‐phosphate dehydrogenase into monomers

Lakatos, Susan; Závodszky, Péter; Elödi, P

doi:10.1016/0014-5793(72)80097-8

Cited by 29 publications

(13 citation statements)

References 9 publications

(8 reference statements)

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“…For WASP, the concentration in the assays was saturating, and for actin filaments it was as high as possible without affecting the viscosity or solubility during the assays. The concentration of actin filaments was two‐fold higher than the maximum reported K d values for aldolase‐actin interactions (0.4–5.0 μM; [Lakatos, Závodszky, & Elódi, 1972; Walsh, Winzor, Clarke, Masters, & Morton, 1980]). Of course, these in vitro concentrations are much diluted from the reported in vivo concentrations of actin (>100 μM [Millard, Sharp, & Machesky, 2004]) and aldolase (6–37 μM [Lundmark & Carlsson, 2003; Orosz et al, 1988; Ottaway & Mowbray, 1977]), but activity assays were performed to assure that binding occurred while the enzyme catalysis was being monitored.…”

Section: Discussionmentioning

confidence: 84%

Actin filament‐ and Wiskott‐Aldrich syndrome protein‐binding sites on fructose‐1,6‐bisphosphate aldolase are functionally distinct from the active site

2020

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The glycolytic enzyme fructose 1,6‐(bis)phosphate aldolase (aldolase) is not only required for efficient utilization of glucose and fructose, but also for cytoskeletal functions like cytokinesis and cell motility. These differing roles are mediated by distinct and discrete binding interactions with aldolase's many binding partners, including actin filaments, Wiskott‐Aldrich Syndrome protein (WASP), and Sorting Nexin 9 (SNX9). How these interactions are coordinated on the aldolase homotetramer of 160 kDa is unclear. In this study, the catalytic activity of wild‐type aldolase is measured in the presence of actin filaments, and a WASP‐derived peptide that binds to aldolase, or both. No appreciable changes in kcat or Km values are seen. Then, aldolase variants with substitutions targeting the tryptophan‐binding pocket for WASP and SNX9 are created and perturbation of actin filament‐, WASP peptide‐, and SNX9 peptide‐binding are assessed. Those that negatively impacted binding did not show an impact on aldolase catalysis. These results suggest that aldolase can engage in catalysis while simultaneously interacting with cytoskeletal machinery.

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Section: Discussionmentioning

confidence: 84%

Actin filament‐ and Wiskott‐Aldrich syndrome protein‐binding sites on fructose‐1,6‐bisphosphate aldolase are functionally distinct from the active site

2020

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“…However, research has been concentrated on evaiuating the activity of oligomeric structures (26)(27)(28). However, research has been concentrated on evaiuating the activity of oligomeric structures (26)(27)(28).…”

Section: Discussionmentioning

confidence: 99%

“…However, research has been concentrated on evaiuating the activity of oligomeric structures (26)(27)(28). A relatively weak perturbation of variables leads to a shift in the T w D t t M equilibria, indicating low stability (small AGdis) of the oligomeric structures [dilution of the enzyme solutions from 10to lo-' M (28), acidification from pH 5 to pH 2 (32), presence of 0.5 M GdnHCl(l1) etc.]. A relatively weak perturbation of variables leads to a shift in the T w D t t M equilibria, indicating low stability (small AGdis) of the oligomeric structures [dilution of the enzyme solutions from 10to lo-' M (28), acidification from pH 5 to pH 2 (32), presence of 0.5 M GdnHCl(l1) etc.].…”

Section: Discussionmentioning

confidence: 99%

Effector‐induced dissociation of glyceraldehyde‐3‐phosphate dehydrogenase discriminated by urea solvation

Иванова

Krusteva

Атанасов

1995

International Journal of Peptide and Protein Research

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The dissociation of glyceraldehyde-3-phosphate dehydrogenase (GAPD) from pig muscle in water solutions (0.1 M phosphate, pH 7) at increased urea concentrations was studied by means of frontal-gel chromatography, intrinsic (TRP) fluorescence, differential absorption spectroscopy and selective chemical modification at TRP-193. The results are in agreement with a consecutive two-step model of dissociation of the tetramer and the dimer ( c t = 0.42 M urea< C b = 1.39 M urea). The binding of effector(s) destabilizes the oligomeric structures (AGT changes from -1.00 to -0.54 kcal/mol; AGD from -2.30 to -1.22 kcal/mol). The introduction of the bulky Koshland-reagent group to TRP-193 at the subunit-subunit interface leads to a decrease of the stability with 6AG x 1 kcal/mol, owing to TRP-193.. .TYR-39.. .TYR-92 cluster destruction. By using lobster GAPD atomic coordinates (PDB file IGPD) and pig muscle GAPD amino-acid sequence, a tentative molecular model was constructed and the subunit contacts in terms of the Lee-Richard static accessibilities were described. A detailed analysis of the dissociation as a transfer of the buried residues from the molecular interface to the urea solutions was performed. 0 Munksgaard 1995.

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“…My first readings were: his excellent review on “Thermodynamic Analysis of Multicomponent Solutions”15 together with Tanford's classical textbook “Physical Chemistry of Macromolecules.”16 This was the time when we studied the association–dissociation equilibrium of enzymes as a function of solvent environment and binding of ligands. The objects of this study were: GAPDH and LDH, both oligomeric allosteric enzymes 17–19. This work was very much related to the analysis performed in Heini's laboratory on glutamate dehydrogenase by Emil Reisler20–22 with the same methodological arsenal which was used by us.…”

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confidence: 99%

Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view

Závodszky

Hajdú

2013

Biopolymers

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To most physicists, it was always evident that conformational fluctuation is an inherent property of all molecules. Its existence in proteins was mentioned first by Linderström-Lang and Schellman in 1959 based on their hydrogen-deuterium exchange experiments. The "induced fit" mechanism to explain ligand-induced conformational changes was suggested by Koshland in 1958. Straub combined these two concepts in his "fluctuation fit" theory in 1964. The era of protein X-ray crystallography imposed a static view of protein structures. With proteins becoming accessible to NMR analysis, conformational dynamics could be mapped, and a new wave of dynamic interpretation of enzymatic catalysis and molecular recognition appeared. Energy landscapes, energy funnels, conformational selection, conformational distribution shifts are now frequent terms in interpreting biomolecular recognition and enzymatic catalysis. All these interpretations are based on the concept that evolution uses the conformational fluctuations of enzymes to develop efficient and dynamic catalytic machines. In a resurrection of the original "fluctuation fit" concept, it is generally recognized now that spatial and temporal events of catalysis are equally important to describe its mechanism. This special issue, dedicated to the memory of Henryk Eisenberg, prompted us to look back at the last 50 years of development of a concept that-like other important concepts-appeared, evolved and became accepted during the period covered by the scientific lifespan of Henryk.

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Dissociation of mammalian D‐glyceraldehyde‐3‐phosphate dehydrogenase into monomers

Cited by 29 publications

References 9 publications

Actin filament‐ and Wiskott‐Aldrich syndrome protein‐binding sites on fructose‐1,6‐bisphosphate aldolase are functionally distinct from the active site

Actin filament‐ and Wiskott‐Aldrich syndrome protein‐binding sites on fructose‐1,6‐bisphosphate aldolase are functionally distinct from the active site

Effector‐induced dissociation of glyceraldehyde‐3‐phosphate dehydrogenase discriminated by urea solvation

Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view

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