. If 20 mM solution of Acetyl-phosphate is transformed to acetate by incubating with a catalytic amoufit of acetate kinase until equilibrium is reached. Acetyl-phosphate Acetate + Pi At equilibrium, the concentration of Acetyl-phosphate is 8 mM. Determine Keq and AG for the hydrolysis of Acetyl-phosphate reaction. (R = 0.008314 kJ/mol · K) ---------

Q: How many ATPs are there in this triglyceride? Showing NADH and FADH2 calculations and steps

A: Triglycerides broken down into glycerol and three fatty acids containing  12, 16 and 14 carbon atom…

Q: The Eo values for the NAD/NADH and Glyceraldehyde-3-phosphate/1,3- Bisphosphoglycerate conjugate…

A: Reduction potential is the potential difference that creates between two species which are reduced…

Q: The kinetics data shown in this graph are from the enzyme lactate dehydrognase, which catalyzes the…

A: The graph that is peesnted is LB plot or Line weaverburk plot.This is a double reciprocal plot where…

Q: Given the following information: 1) Glucose-6-Phosphate → 2) culate BOTH AG! AND K'eq for the…

A: Gibbs free energy is the amount of energy, which is used to perform several other functions.

Q: In the cytosol of rat hepatocytes, the temperature is 37 °C and the mass-action ratio, Q, is…

A: Temperature = 37 degree Celsius                          = 273 + 37 = 310 k mass action ratio (Q) =…

Q: You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of…

A: LDH measurements are used  in the daignosis abd treatment of luver diseases such as acute viral…

Q: a) You evaluate the lipoxygenase inhibition by different concentrations of octyl protocathechuate.…

A: Inhibitors are the substances that bind to enzymes to regulate their activity . There are…

Q: Calculate the values of the

A: Enzyme kinetics is a study of the rate of enzyme catalyzed reactions. In Michaelis-Menten kinetics,…

Q: . For parts (a) and (b) of this problem use the following standard reduction potentials, free…

A: The equilibrium constant of a chemical reaction is the value of its reaction quotient at chemical…

Q: For the competitive, noncompetitive and uncompetitive inhibition type investigate following figures…

A: The enzyme inhibition is the regulatory mechanism of the enzyme. They are of two types, irreversible…

Q: If the Gibbs free energy change for the reaction; Succinate + FAD Fumarate + FADH2 is -40KJ/mol at…

A: Biological oxidation-reduction reactions involve the transfer of electrons from one biomolecule,…

Q: 41 The following data describe an enzyme-catalyzed reaction (hydrolysis of…

A: We are authorized to answer three subparts at a time, since you have not mentioned which part you…

Q: Determine the type of inhibition by AMP? Explain

A: Inhibitors are substances which inhibit the enzyme activity by binding to the active site or…

Q: Calculate the standard-state free energy change for the isomerization of glucose-1-phosphate to…

A: Introduction: The isomerization of glucose 1-phosphate to glucose 6-phosphate is catalyzed by the…

Q: Discuss how the equation for enzymatic reaction (given below) was demonstrated in the experimental…

A: Enzymes are biocatalysts, and they are involved in increasing the rate of the reaction. They are…

Q: Km V. (V) 15) + V = [S] max a' = 2 a' = 1.5 (7) -15⁰° max a Vmax 1 [S] MM a'=1 [1]

A: Most of the enzymes have certain kinetic properties. whenever a substrate is added to them, the…

Q: phosphoserine + H2O → serine + Pi Kinetics measurements were performed using a range of Mg**…

A: Inhibition: A substance that decreases or slows down the activity of other substances is known as an…

Q: In muscle cells, the AG for glucose+ATP = glucose– 6–P+ADP is –33.5 kJ·mol-1. In contrast, the AG…

A: During glycolysis, Glucose is converted into Pyruvate. The first step of glycolysis is the…

Q: At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40…

A: Introduction Enzymes increase the rate of a chemical reaction several times as compared to an…

Q: For the reaction glutamate (aq) + oxaloacetate²- (aq) a-ketoglutarate2- (aq) + aspartate¯ (aq) the…

A: Standards free energy change calculated at biochemical standards is called biochemical standard free…

Q: calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: WHAT IS THE asmoTIC PRESSURE OF A SOLUTION OF BOVINE IinsuLIN (MOLAR MASS 5700g mol - 1 ) at 100.0…

A: Movement of solvent from a solution of lower concentration to the solution of higher concentration…

Q: The drug troglitazone was used to treat diabetes but was withdrawn from the market when patients who…

A: Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…

Q: Standard redox potentials E' for some common compounds in biochemistry: Eo' (Volt) + 0,81 12 O2 + 2…

A: If the Gibbs free is negative for  a reaction then the process is said to be spontaneous. A positive…

Q: Referring to for E′0 values, calculate ΔG°′ for oxidation of malate by malate dehydrogenase.

A: Standard free energy change of reaction symbolized as ΔG°′ is a thermodynamic measure used to denote…

Q: Many enzymes obey simple Michaelis–Mentenkinetics, which are summarized by the equationrate = Vmax…

A: Michaelis-Menton kinetics is an equation that describes the rate of enzymatic reactions by relating…

Q: Calculate the equilibrium concentration of H2O for the following esterification reaction performed…

A:

Q: The maximum saturation, 28.3ug of enzyme in 25ml water catalyzes the oxidation of ethanol at a rate…

A: Introduction Catalytic constant, also known as the turnover number can be given as kcat=v[Et]where v…

Q: at what substrate concentration is v= 5.0 mM s^-1 for the enzyme catalyzed hydrolysis of trehalose?

A: 1 molecule trehalose is hydrolyzed into 2 glucose molecules by the trehalase enzyme.

Q: A) Calculate the Gibbs free energy change for the following reaction: Fructose diphosphate If the…

A: Gibbs free energy, denoted G, combines enthalpy & entropy into a common value. The change in…

Q: Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of…

A: In chemical and especially biochemical systems (like cells), we are concerned more about the energy…

Q: A +B C+D 1) Calculate AG for the above reac un and indicáte whether the reaction is favorable or…

A: Gibb's free energy∆G: It determines whether the given reaction will be Spontaneous or…

Q: Acetaldehyde + NADH + H+ → Ethanol + NAD+ How is the inhibition constant for this gotten? Determine…

A: The enzyme is a biomolecule that catalyzes the reaction by binding to the…

Q: does this is inhibitor  good to use to inhibit toxanthine oxidase in the case of hyperuricemia and…

A: Human xanthine oxidase is an enzyme, which catalyzes the oxidation of hypoxanthine to xanthine and…

Q: Substrate Concentration (mol L-1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526…

A: Lineweaver-Burk plot also known as the double reciprocal plot is used to graphically represent the…

Q: Construct a graph of the rate of reaction as a function of PNPA concentration for the…

A: we have to plot graph between trypsin rate and pNPA.

Q: Calculate K’eq and ΔG’0 for the following: A 0.1 M solution of glucose 1-phosphate at 25oC is…

A: Keq is the equilibrium constant and it is a measure of ratio of concentration of products to…

Q: at R #314 J K not

A: Catalytic efficiency of enzymatic reaction (turnover)For catalysed reaction the Kcat is used where…