In glycolysis, fructose 1,6-bisphosphate is converted to two products with a standard free- energy change (AG) of 23.8 kJ/mol. Under what cellular conditions will the free-energy change be negative, enabling the reaction to proceed spontaneously to form products? O In a cell where the concentrations of products and reactants yield a low value of the mass-action ratio Q ○ The reaction will not go to the right spontaneously under any conditions because the AG is positive ○ The reaction will proceed spontaneously to the right if there is a high concentration of products relative to the concentration of fructose 1,6-bisphosphate ○ The reaction will proceed spontaneously to the right if there is a high concentration of enzyme to catalyze the reaction O None of these conditions is sufficient

Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]

1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0.   c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?

You begin to study enzyme Z, which catalyzes a simple reversible reaction that interconverts compound S and compound P. You observe that the ∆G´° for the S to P conversion to be –6 kJ/mol, and that compound S has ∆G´° for binding to enzyme Z of –15 kJ/mol, while compound P has a ∆G´° for binding to enzyme Z of –13 kJ/mol. Please explain the effect of enzyme Z on conversion of S to P. (Your answer should include a graph qualitatively  showing energy versus reaction progress; however, you still need to explain youranswer in words!) not sure how to make the correct graph.

The following nutrient molecule is digested and transported to a cell where it undergoes further catabolism: но c-(CH;)14-CH3 di In the table below, list the important products of the complete B oxidation of this molecule. • In the first column of the table, write the chemical formula, name, or standard biochemical symbol for a product molecule. In the second column, write the total number of these molecules produced. • Only list the Important products, including (1) molecules with any of the carbon atoms that were in the original molecule, (2) energy storage molecules (like ATP), and (3) newly oxidized or reduced coenzymes. List each product molecule on a separate row. You can add more rows if you need them. • Be sure you write the number of product molecules formed by the complete B oxidation of the molecule above. • Do not include the products of any catabolic activity that happens before or after B oxidation, including any necessary activation. If the molecule contains small parts…

When 10 micrograms of an enzyme with a molecular mass of 80,000 Daultons (grams/mol) is added to a solution containing its substrate at a concentration 100 times the Km, it catalyzes the conversion of 65 micromoles of substrate into product in 3 minutes. What is the enzyme's turnover number (in units of min-1)?

A particular reaction has a ΔG‡ of 30.0 kJ mol-1 at 25.0 °C. In the presence of an enzyme, the same reaction has a ΔG‡ of 1.50 kJ mol-1 at the same temperature. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)

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a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.

Consider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 23.7, and the temperature is 37.0 °C? AG" for the reaction is -16.7 kJ/mol. The constant R = 8.3145 J/(mol-K) AG= Number kJ/mol