mutations in adenylate kinase have led to a hyperactive enzyme that ultimately ends up elevating adp levels in a cell. calculate Ec given the following atypical adenylate concentrations for the cell containing atp: .o5 mM adp 12.2mM and amp 80micromole

Mutations in adenylate kinase have led to a hyperactive enzyme that ultimately ends up elevating ADP levels in a cell.Calculate the EC (energy charge) given the following atypical adenylate concentrations for the cell containing the mutant adenylate kinase: ATP = 0.5 ??��, ADP = 12.2 ??��, AMP = 80 ??��.

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?

ΔG°′ for the aldolase reaction is 22.8 kJ · mol−1. In the cell at 37°C, [DHAP]/ [GAP] = 5.5. Calculate the equilibrium ratio of [FBP]/[GAP] when [GAP] = 10−4 M.

Discuss two approaches (methods) based on week-intermolecular forces on detection of ATP over AMP? please explain, hand written answer will be preffered, thanks

Give all the reactions that will produce ATP either by substrate-level phosphorylation (SLP) or by oxidative phosphorylation (OP). If the given require a shuttle system, please indicate both MA shuttle and GP shuttle and give the ATP produced.  Given: fructose 6-phosphate to 2pyruvate

Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.

Describe the categories of enzyme control: (image provided) Allosteric control with example Covalent modification with example

In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?

n your own words and with your own diagrams, describe the catalytic reaction mechanism of the enzyme acetylcholinesterase. Discuss the functional roles of each member of the catalytic triad plus whatever other residues that you find important. Describe the actual movements of protons, and the making and breaking of bonds. What types of chemistries is the enzyme using? (what is the enzyme doing, in term of reaction