What are the description of the ff? A. Enzyme influence on reaction velocity B. Effect of temperature on enzymatic activity
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What are the description of the ff?
A. Enzyme influence on reaction
velocity
B. Effect of temperature on
enzymatic activity
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Solved in 2 steps
- What are the description of the ff?A. Effect of pH with enzymaticactivity. Include example ofenzymes optimum pH.B. Effect of activators on theactivity of enzymes. Includeexamples.A biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme Bwhat are correct about enzyme kinetic parameters
- Compare the KM and Vmax of the enzyme in the absence and presence of inhibitors to determine what type of inhibitors are compounds Y and Z. Explain your answers.Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.How does the average reaction rate differ from an instantaneous reaction rate? © A. The average reaction rate is how quickly the reaction proceeds over time. An instantaneous reaction rate is how quickly the reaction proceeds at a specific time. B. The average reaction rate is how quickly the reaction proceeds at a specific time. An instantaneous reaction rate is how quickly the reaction proceeds over time. C. The average reaction rate is how quickly the reaction proceeds over time considering the reactants. An instantaneous reaction rate is how quickly the reaction proceeds at a specific time considering the products. D. The average reaction rate is how quickly the reaction proceeds over time. An instantaneous reaction rate is how quickly the reaction proceeds compared to another reaction.
- state a optimum temperature of enzyme EWhat is the qaulitative abstract for Color Reactions of Proteins and Amino Acids? (one paragraph only) Please follow this format for writing an abstract:-In one paragraph a. Problem studied or purpose of the activity b. Example approach c. Summarize the major findings d. major conclusionIdentify the type of enzyme inhibition each of the following inhibitor characteristics is associated with: 1. An inhibitor that decreases enzyme activity by binding to a site on the enzyme other that the active site. 2. An inhibitor that inactivates enzymes by forming a strong covalent bond of the enzyme acitve site.
- A medicinal chemist is trying to determine the mechanism of action of inhibitors she has synthesized. The relative change in KM and Vmax upon incubation of the targeted enzyme with each inhibitor is shown in the table below. Inhibitor A Inhibitor B Inhibitor C Using this data, the mechanism of action of Inhibitor C is: Uncompetitive TS‡ analog Mixed Inhibition Competitive Кмарр- Км 0 Non-competitive app - Vmax <0 <0 0 VmaxSucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…If a competitive inhibitor of an enzyme is added to the mixture of the enzyme and its substrate, the inhibitor will: O a. decrease the value of Vmax for the chemical reaction catalyzed by this enzyme O b. decrease the value of KM for the chemical reaction catalyzed by this enzyme O c. increase the value of KM for the chemical reaction catalyzed by this enzyme O d. increase the value of Vmax for the chemical reaction catalyzed by this enzyme