From your Lineweaver-Burk plot, derive the values for the following table. Indicate the appropriate units. (b) By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.   Km Vmax Uninhibited     Inhibited

Q: 3. Draw the structure of the catalytic triad found in the active site of chymotrypsin and explain…

A: Lineweaver Burk (LB) plot has 1/v0 as Y-axis and 1/[S0] as X-axis. Competitive, Uncompetitive and…

Q: Shown below is Lineweaver-Burk plot for an enzymatic reaction at different substrate concentrations…

A: Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction…

Q: change for formation of an ES complex if the KD for this enzyme/ligand pair is 0.28µM? Give your…

A: The free energy change (ΔG) for the formation of an ES complex can be calculated using the…

Q: Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal…

A: Lineweaver-Burk plot is the graphical representation of Lineweaver-Burk equation which is a double…

Q: Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten…

A: The Michaelis- Menten equation is an equation used to predict the rate of product formation of a…

Q: Vmax and Km were calculated for enzyme substrate data. Results Y=0,0063x+0,3929 Km =62,4 mikromol/L…

A: From the LB plot of enzyme kinetics, y=mx+c  It's an equation of a straight line. 1/V=(Km/Vm )1/S…

Q: glucose to form glucose-6-phosphate shown below. The net AG° for this reaction is glucose phosphate…

A: The strategy of coupled reaction is employed by all living cells in the synthesis of metabolic…

Q: Án enzyme that follows Michaelis-Menten kinetics has a KM value of 3.00 µM and a kat value of 181s1.…

A: An enzyme is a type of biological catalyst that aids in the acceleration of chemical reactions.…

Q: enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 μM and a kcat value of 206 s−1…

A: This is about enzyme kinetics and the questions related to it Given values- Km = 0.0100 μM kcat =206…

Q: If the hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase has a ΔG′∘ of…

A: In a general reaction such as: aA + bB ⇌ cC + dD At equilibrium (steady state), the concentration of…

Q: An enzyme has a rate enhancement of 1.3x106. Calculate the value of ΔΔG‡ at 25.0 °C in kJ mol-1.…

A: Step 1: Step 2: Step 3: Step 4:

Q: [S, mmol L-') Vo (umol L-' min-') 0.5 50 1.0 2.0 3.0 10.0 8||||

A: Given values; Km of the enzyme = 1 mM At S1= 0.5 mM, Vo = 50 μmol/min S2 = 1 mM, Vo=? S3 = 2 mM ,…

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: The change in the amount of product B in a reaction which is catalyzed by Enzyme A is given in the…

A: Michaelis menten constant, Km= It is the substrate concentration required to produce half maximum…

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: Given the following information about an enzymatic reaction, calculate the initial velocity. Your…

A: The Michaelis–Menten kinetics of an enzymatic reaction shows the relation between the substrate…

Q: Use the data below to determine the maximum velocity [in mM/s] of a certain enzyme-catalyzed…

A: We must know the Michaelis Menten equation: V=Vmax [S]Km+ [S]

Q: The enzyme β-methylaspartase catalyzes the deamination of β-methylaspartate. For this aspartate…

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

Q: During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic…

A: If a reaction velocity v/s substrate concentration curve shifts to the right, then the curve becomes…

Q: The rates at various substrate conce are recorded as follows: (b) 2.5 5.0 10.0 15.0 IS]/10 M 2.2 3.8…

A: The Michaelis-Menten equation tells the relationship between the initial rate of an enzymatic…

Q: The following kinetic data were obtained for an enzyme in the absence of an inhibitor (1) and in the…

A: The determination of Vmax and KM for any enzyme kinetic reaction requires the plotting of the data…

Q: Glucose 6-phosphate Glucose 1-phosphate After reactant and product were mixed and allowed to reach…

A: Glucose-6 phosphate is the 1st intermediate of the process of glucose metabolism. It plays a major…

Q: From a kinetics experiment, Kcat was determined to be 55sec^-1. For the kinetic assay, 0.05mL of a…

A: The concentration of enzyme stock solution was 0.05mg/ml. i.e. 1ml contain 0.05mg of enzyme. We took…

Q: Draw a hypothetical Michaelis-Menten plot for an enzyme reaction (i) without and (ii) with a pure…

A: Enzymes are the class of proteins that elevates the rate of the chemical reaction within the living…

Q: At what substrate concentration would an enzyme with a kcat of 33.0 s-1 and a Km of 0.0046 M operate…

A: The Michali s-Menten kinetics is enzyme kinetics that is common in biochemistry to detect and…

Q: The table below lists experimental conditions that can be applied to a reaction catalyzed by a…

A: Enzymes are the biocatalyst that can increase the rate of biochemical reaction without itself being…

Q: (i)  Which graph indicates an enzymatic reaction without inhibitor?(ii)  Which type of inhibitor is…

A: The y-intercept in the graph indicates 1/Vmax. The x-intercept in the graph indicates -1/km. A low…

Q: Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the…

A: Vmax : Reaction rate- when the enzyme gets fully occupied by substrate. Vmax- Maximum velocity

Q: Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the…

A: The change in Gibbs free energy ∆G0 is a thermodynamics potential that is used to calculate the free…

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: Lysozyme is a catalytic enzyme that cleaves NAG-NAM units in the bacte- rial cell wall, and is found…

A: Lysozyme is a naturally occurring enzyme found in secretions such as tears, saliva and milk. It…

Q: (a) If the total enzyme concentration  1 nmol/L, how many molecules of substrate can a molecule of…

A: Given Values: Concentration of enzyme in each cases represented in the question = 1 nmol/L

Q: Calculate the Km of the enzyme with these parameters.  kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM…

A: Km of an enzyme is known as Michalis constant, which denotes the substrate concentration at which…

Q: When 10 micrograms of an enzyme with a molecular mass of 80,000 Daultons (grams/mol) is added to a…

A: Before going into the calculations for finding the turnover number (kcat), we need to convert…

Q: Estimate the Km and Vmax in the absence and in the presence of inhibitors Determine what type of…

A: Michaelis menten constant, Km= It is the substrate concentration required to produce half maximum…

Q: The Lineweaver - Burk plot (Figure 1) shows an enzyme-catalyzed reaction in the absence and presence…

A: In a lineweaver burk plot, x intercept represents the negative reciprocal of Km and y axis…

Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…

A: The rate of a enzyme catalyzed reaction increases with temperature until a point and once the…

Q: Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X.…

A: Line-weaver Burk plot is also known as double reciprocal plot and is modification of…

Q: In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC…

A: Vmax km Competitive   remains same increases Non Competitive  Decreases remains same…