Dimethylsulfoxide promotes K+-independent activity of pyruvate kinase and the acquisition of the active catalytic conformation

European Journal of Biochemistry

Volumn 268, Issue 11, 2001, Pages 3267-3274

  Ramírez Silva, Leticia ^a   Ferreira, Sérgio T ^b   Nowak, Thomas ^c   De Gómez Puyou, Marietta Tuena ^d   Gómez Puyou, Armando ^d  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c UNIVERSITY OF NOTRE DAME   (United States)

^d UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

Author keywords

Catalytic conformation; Cosolvents; Dimethylsulfoxide; Pyruvate kinase

Indexed keywords

APOENZYME; DIMETHYL SULFOXIDE; MAGNESIUM; PHOSPHOENOLPYRUVATE; POTASSIUM; PYRUVATE KINASE; SOLVENT; WATER;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITION; MICELLE; NONHUMAN; PRIORITY JOURNAL;

BINDING SITES; CATALYSIS; CATIONS, MONOVALENT; DIMETHYL SULFOXIDE; ENZYME ACTIVATION; HYDROGEN-ION CONCENTRATION; POTASSIUM; PROTEIN CONFORMATION; PYRUVATE KINASE; SOLVENTS; WATER;

EID: 0034844439     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02222.x     Document Type: Article

References (54)

1. Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase
2. Thallium (I) activation of pyruvate kinase
3. Conformational changes required for pyruvate kinase activity as modulated by monovalent cations
4. Use of protein difference spectrophotometry to determine enzyme-cofactor dissociation constants
5. Effects of temperature, substrates, and activating cations on the conformations of pyruvate kinase in aqueous solutions
6. Studies on the interaction of substrate and monovalent and divalent cations with pyruvate kinase
7. Effects of univalent cations on the immunoelectrophoretic behavior of pyruvic kinase
8. Kinetics and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates
9. Thallium-205 nuclear magnetic resonance as a probe for studying metal ion binding to biological macromolecules. Estimate of the distance between the monovalent and divalent activators of pyruvate kinase
10. Nuclear magnetic resonance studies of the function of potassium in the mechanism of pyruvate kinase
11. A multinuclear nuclear magnetic resonance study of the monovalent-divalent cation sites of pyruvate kinase
12. +, and pyruvate
13. +, and L-phospholactate at 2.7 Å resolution
14. 2+-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 Å resolution: ATP binding over a barrel
15. The allosteric regulation of pyruvate kinase by fructose-1,6-biphosphate
16. Crystal structure of Escherichia coli pyruvate kinase type I: Molecular basis of the allosteric transition
17. The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity
18. +requirements for the activity of pyruvate kinase entrapped in reverse micelles
19. +
20. High affinity binding of monovalent Pi by beef heart mitochondrial adenosine triphosphatase
21. A purification of brewers' and bakers' yeast enolase yielding a single active component
22. Pyruvate kinase from muscle
23. CHELATOR: An improved method for computing metal ion concentrations in physiological solutions
24. Magnetic resonance studies of the interaction of the manganous ion with bovine serum albumin
25. Nuclear relaxation studies of ligand-enzyme interactions
26. Characterization of the second metal site on avian phosphoenolpyruvate carboxykinase
27. Subunit structure of rabbit muscle pyruvate kinase
28. Molecular weight and quaternary structure of lactic dehydrogenase. 3. Comparative determination by sedimentation analysis, light scattering and osmosis
29. The thermodynamic properties of aqueous solutions of polyethylene glycol, polyprolyne glycol and dioxane
30. A large enhancement of solvation enthalpy by the reduction of temperature
31. Enzymology in aqueous-organic cosolvent binary mixtures
32. 2O
33. Relevance of dielectric constant and solvent hydrophobicity to the organic solvent effect in enzymology
34. Change of water structure by solvents and polymers
35. Lysozyme kinetics in low water activity media. A possible hydration memory
36. Role of water in the energy of hydrolysis of phosphate compounds - Energy transduction in biological membranes
37. Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
38. Effect of inert polymers on protein self-association
39. Polymer-protein interactions. Comparison of experiment and excluded volume theory
40. Mechanism of poly (ethylene glycol) interaction with proteins
41. Contribution of the surface free energy perturbation to protein-solvent interactions
42. Beware of proteins in dimethylsulfoxide
43. Remarkable activation of enzymes in nonaqueous media by denaturing organic solvents
44. Effects of organic solvents on protein structures: Observation of a structured helical core in hen egg-white lysozyme in aqueous dimethyl sulfoxide
45. Characterization of the structural and functional changes of hemoglobin in dimethyl sulfoxide by spectroscopic techniques
46. The structure of cat muscle pyruvate kinase
47. Effects of temperature and activating cations on the fluorescence of pyruvate kinase
48. Magnetic resonance studies of metal activation of enzymic reactions of nucleotide and other phosphate substrates
49. Influence of polyethylene glycols on the kinetics of rat liver phosphofructokinase
50. Effect of the polyethylene glycol on the kinetic behaviour of pyruvate kinase and other potentially regulatory liver enzymes
51. Modulation of muscle phosphofructokinase at physiological concentration of enzyme
52. Subunit interactions of Rubisco activase: Polyethylene glycol promotes self-association, stimulates ATPase and activation activities, and enhances interactions with Rubisco
53. Activation of cytosolic pyruvate kinase by polyethylene glycol
54. The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117