Kinetic measurements on the pyruvate kinase reaction in erythrocytes

1979 ◽  
Vol 38 (2) ◽  
pp. 169-173 ◽  
Author(s):  
M. Lakomek ◽  
W. Schr�ter ◽  
H. Winkler
Keyword(s):  
Pyruvate Kinase ◽  
Kinetic Measurements ◽  
Kinase Reaction

scholarly journals Kinetic and Magnetic Resonance Studies of the Pyruvate Kinase Reaction

1965 ◽  
Vol 240 (1) ◽  
pp. 238-246 ◽  
Author(s):  
Albert S. Mildvan ◽  
Mildred Cohn
Keyword(s):  
Magnetic Resonance ◽  
Pyruvate Kinase ◽  
Magnetic Resonance Studies ◽  
Kinase Reaction

Free energy dissipation of the pyruvate kinase reaction has a minimum at cell metabolite concentrations

1983 ◽  
Vol 18 (4) ◽  
pp. 349-352
Author(s):  
Mario Markus ◽  
Theodor Plesser
Keyword(s):  
Free Energy ◽  
Energy Dissipation ◽  
Pyruvate Kinase ◽  
Kinase Reaction ◽  
Metabolite Concentrations

Stereochemical studies of the pyruvate kinase reaction with (Z)- and (E)-phosphoenol-α-ketobutyrate

Biochemistry ◽  
1977 ◽  
Vol 16 (20) ◽  
pp. 4382-4387 ◽  
Author(s):  
Mella Adlersberg ◽  
Jean Dayan ◽  
William E. Bondinell ◽  
David B. Sprinson
Keyword(s):  
Pyruvate Kinase ◽  
Kinase Reaction

A rate-determining proton relay in the pyruvate kinase reaction

Biochemistry ◽  
1991 ◽  
Vol 30 (3) ◽  
pp. 722-726 ◽  
Author(s):  
Irwin A. Rose ◽  
Donald J. Kuo ◽  
Jessie V. B. Warms
Keyword(s):  
Pyruvate Kinase ◽  
Kinase Reaction ◽  
Proton Relay

scholarly journals Studies on the cyclic 3':5'-AMP-stimulated pig liver protein kinase reaction with pyruvate kinase as substrate.

1977 ◽  
Vol 252 (2) ◽  
pp. 613-619
Author(s):  
L Berglund ◽  
O Ljungström ◽  
L Engström
Keyword(s):  
Protein Kinase ◽  
Pyruvate Kinase ◽  
Liver Protein ◽  
Pig Liver ◽  
Kinase Reaction

Substrate proton of the pyruvate kinase reaction

Biochemistry ◽  
1989 ◽  
Vol 28 (25) ◽  
pp. 9579-9585 ◽  
Author(s):  
Irwin A. Rose ◽  
Donald J. Kuo
Keyword(s):  
Pyruvate Kinase ◽  
Kinase Reaction

scholarly journals The adenosine triphosphate inhibition of the pyruvate kinase reaction and its dependence on the total magnesium ion concentration

1969 ◽  
Vol 112 (3) ◽  
pp. 303-316 ◽  
Author(s):  
Holm Holmsen ◽  
Eva Storm
Keyword(s):  
Hydrochloric Acid ◽  
Sodium Hydroxide ◽  
Pyruvate Kinase ◽  
Reaction Rate ◽  
Reaction Rates ◽  
Magnesium Concentration ◽  
Trimethylammonium Chloride ◽  
Maximal Rate ◽  
Acid System ◽  
Kinase Reaction

1. The effects of ATP, PPi and EDTA on the skeletal-muscle pyruvate kinase reaction at various concentrations of magnesium (where ‘magnesium’ refers to total Mg2+, both free and in the form of complexes) were investigated. The reaction rate was determined as the amount of pyruvate formed in a recorded time of incubation. 2. At 44mm-magnesium the Km values for ADP and phosphoenolpyruvate were unaltered by the presence of ATP up to 6·8mm in systems buffered with either tris–hydrochloric acid or glycylglycine–sodium hydroxide, but the Km values were different in these systems. The Km for one substrate was independent of the concentration of the second substrate. 3. At 10mm-magnesium in the tris–hydrochloric acid system ATP inhibited the reaction competitively with respect to ADP and phosphoenolpyruvate. In the glycylglycine–sodium hydroxide system the inhibition appeared to be non-competitive. At 10mm-magnesium the Km values were lower than at 44mm-magnesium and dependent on the system used. 4. In the tris–hydrochloric acid system the reaction rate rose with increasing magnesium concentration up to a maximum at a concentration 10–20 times that of ADP. Further increase inhibited the reaction and at 44mm-magnesium the rate was 25–50% of its maximum. This inhibition paralleled that produced by increasing trimethylammonium chloride concentrations and was not due to a specific effect of the Mg2+ ion. 5. In the presence of 6·8mm-ATP no reaction occurred below 4–6mm-magnesium, and further increase apparently abolished the inhibition as the reaction rate increased and became equal to those obtained in the absence of ATP at 10–25mm-magnesium. Further increase in magnesium concentration gave reaction rates that were slightly higher in the presence of ATP than in its absence. The maximal rate in the presence of ATP was distinctly lower than in its absence. When 6·8mm-PPi or 6·8mm-EDTA was present the variations in reaction rate with rising magnesium concentration were similar to that obtained in the presence of ATP below 6–8mm-magnesium but further increase in the magnesium concentration resulted in an increase in the rate up to a maximum comparable with that of the control. The effect of pure chelation was thus a displacement of the reaction maximum to higher magnesium concentrations without changing the maximal rate. When correction had been made for this effect, ATP gave inhibition at 44mm-magnesium that was competitive with respect to ADP (Ki 2·1×10−2m). This degree of inhibition is far less than was reported earlier and its importance for the mechanism of the pyruvate kinase reaction is discussed.

scholarly journals 31P NMR of the pyruvate kinase reaction: An undergraduate experiment in enzyme kinetics

2017 ◽  
Vol 45 (6) ◽  
pp. 509-514 ◽  
Author(s):  
R. Marshall Werner ◽  
Austin Johnson
Keyword(s):  
Enzyme Kinetics ◽  
Pyruvate Kinase ◽  
31P Nmr ◽  
Kinase Reaction

scholarly journals Thermodynamics of the Pyruvate Kinase Reaction and the Reversal of Glycolysis in Heart and Skeletal Muscle

2002 ◽  
Vol 277 (30) ◽  
pp. 27176-27182 ◽  
Author(s):  
Geoffrey P. Dobson ◽  
Sam Hitchins ◽  
Walter E. Teague
Keyword(s):  
Skeletal Muscle ◽  
Pyruvate Kinase ◽  
Kinase Reaction
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