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- Allosteric regulation O The product of a series of reactions acts as an inhibitor for an earlier reaction. O Hormones control the synthesis of enzymes. A regulator binds to the enzyme at a site other than the active site. This binding changes the shape of the enzyme and alters the catalytic ability of the enzyme. An inhibitor binds reversibly to the enzymesubstrate complex, blocking the binding of the second substrate to the active site. The activity of an enzyme is influenced by the addition or removal of a group that is covalently bonded to the enzyme. O An inhibitor forms covalent bonds to the active site. permanently blocking it.X Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.Graph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.
- Enzyme Properties The effect of temperature on enzyme activity. Temperature °C 10 Reaction rate 1.0 15 1.5 20 2.5 25 3.5 30 5.5 35 7.5 40 9.5 45 50 8.5 7.0 55 4.0 60 0.0 a. "DRAW A LINE GRAPH OF THE RESULTS OF THE EFFECTS OF TEMPERATURE ON A TYPICAL ENZYME REACTION RATE." b. WHAT IS THE BEST TEMPERATURE FOR THIS ENZYME TO WORK? c. MOST ENZYMES WORK AT THIS TEMPERATURE IN HUMANS, WHY DO YOU THINK THIS IS?USSE EUSS reaction rate substrate concentration Blue line - Enzyme alone Red line - Enzyme + unknown compound The 4 graphs above represent the change in enzyme kinetics with the individual addition of different compounds that could be categorized as either: allosteric inhibitors, allosteric activators, competitive inhibitors, activators or non-competitive inhibitors. Review the graphs above. Each graph represents the activity of an enzyme and the enzyme + the addition of an unknown compound. By comparing the kinetics of the enzyme alone to the enzyme + unknown, determine what type of compound was added to each of the 4 different solutions to elicit the observed change.The classic concept of bond strain is more correctly described in what way? Select the correct response: The transfer of electron from one chemical moiety to another results to decrease in steric hindrance. The chemical bonds of the substrate is distorted due to the presence of metal ions in the vicinity of the active site. The transition state makes better contact with the enzyme than the substrate due to stabilization effect of various moieties in the active site. The electron cloud of the substrate is polarized by more electronegative moieties in the active site.
- Enzyme specificity (list the different types of enzyme specificities)advantages and disadvantages of enzyme inhibition. With explainAllosteric Inhibitors ● are constructed of level of protein polypeptide chains (demonstrating on each polypeptide. structure) with an ● The enzyme moves back and forth between an active state and an inactive state ● If a substance binds to the allosteric site and puts the enzyme into the active state, that substance is called an ● If a substance binds to the allosteric site and puts the enzyme into the inactive state, that substance is called
- Understanding how enzymes work 1) Excluding enzymes, for example, that work in the stomach's low pH, describe the working conditions for most enzymes in the human body. 2) Describe the effect of enzymes on the rate of reactions that they catalyze. 3) Define the transition state in a chemical reaction and how an enzyme functions during the transition state.True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.