How do I draw a diagram for Phosphoenolpyruvate (PEP) + ADP → Pyruvate + ATP to show the effect of the enzyme on reaction rate?

For : Phosphoenolpyruvate (PEP) + ADP → Pyruvate + ATP - how do I tell if it is exergonic or endergonic?

From data in the table, calculate the AG'º value for the reactions. Reaction AG° (kJ/mol) Phosphocreatine + H,O → creatine + P; |-43.0 |ADP + P; → ATP + H,O |+30.5 Fructose + P; → fructose 6-phosphate + H,0 +15.9 Phosphocreatine + ADP → creatine + ATP AG'º = kJ/mol ATP + fructose → ADP + fructose 6-phosphate AG'º = kJ/mol

Analyze the reaction below and identify the major class of enzyme that catalyzes the the given reaction:

The phosphorylation of glucose to glucose 1-phosphate requires 5.0 kcal/mol of energy. This unfavorable reaction can be driven by the hydrolysis of ATP to ADP. (a) Write the equation for the coupled reaction. (b) How much energy is released in the coupled reaction? glucose + HPO4---------->2– glucose 1-phosphate + H2O

Indicate whether each of the following changes represents oxidation or reduction. Write: O = for oxidation ; R= for reduction Example: cyt ci (Fet) → cyt c1 (Fe2+) Answer: R Blank #1: COQH2 → CoQ Blank #2: NAD+ - NADH Blank #3: FMN → FMNH2 Blank # 4: FADH2 FAD Blank #5: Fe(III) SP → Fe(II) SP Blank # 1 Blank # 2

If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for sucrose synthesis from glucose + fructose is +5.5 kcal/mole, calculate standard free energy change for the combined reaction of ATP + glucose + fructose g ADP + sucrose + inorganic phosphate. DGo = -12.8 kcal/mole DGo = -1.8 kcal/mole DGo = 0 kcal/mole DGo = +1.8 kcal/mole DGo = +12.8 kcal/mole

The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinate

Discuss the composition of the transition state for the formation of ATP by ATP Synthase. a) Where is the active site for this enzyme located? b) How are the amino acid side chains from the α and β subunits of ATP Synthase involved? c) Discuss the importance of Mg+2 in the mechanism of this enzyme.

What terms would best describe the above coupled reaction? (If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for maltose synthesis from glucose + glucose is +3.7 kcal/mole, calculate the standard free energy change for the combined reaction of ATP + glucose + glucose g ADP + maltose + inorganic phosphate.) it is non-spontaneous and endothermic (because the overall DGo is negative) it is spontaneous and exothermic (because the overall DGo is negative) it is non-spontaneous and endothermic (because the overall DGo is positive) it is spontaneous and exothermic (because the overall DGo is positive) it is non-spontaneous and exothermic (because the overall DGo is negative)