The best conditions under which the enzyme chymotrypsin functions are
i) pH = 7.8
ii) Temperature = 50 oC
-Chymotrypsin is completely inhibited by 10 mM Cu2+ and Hg2+.
The typical range for the Michaelis-Menten constant of Chymotrypsin is KM = 15 mM
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
biochemistry class homework Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a variety of mechanisms. These mechanisms generally utilize strategies such as improving the nucleophiles and electrophiles present in the catalytic R groups or substrates, stabilizing the extra electron density of the leaving group, and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease...
2. List some familiar adaptations animals have to reduce the effects of temperature extremes on their many vital, enzyme-catalyzed reactions. 3. In general, the rates of chemical reactions double for every 10 degrees (Celsius) increase in temperature. What changes at the molecular level account for slower reaction rates of enzyme- catalyzed reactions at high temperatures? (Hint: enzymes are protein molecules. What happens to protein molecules when they are heated?) Why are enzyme catalyzed reactions also slower at low temperatures? (Hint:...
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a wide variety of mechanisms. These mechanisms generally utilize the following strategies: improving the nucleophiles and electrophiles present in the catalytic R groups or substrates; stabilizing the extra electron density of the leaving group; and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease found in...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not existade without the presence of enzymes. Enzymes increase reaction rates through a wide variety of mechanisms These mechanisms generally utilize the folowing strategies: improving the nucleophiles and electrophiles present in the catalytic R groups or substrates; stabilizing the extra electron density of the leaving group; and stabilizing transition states Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a pryodeoph bic amino...
1 2 3 4 5 6 7 8 9 Part A Which of the following is/are means whereby a catalyst can lower the activation energy of a reaction? quantum tunneling decreasing the number of reactive molecules permanently binding substrates inefficient collisions altering the temperature within the cell to one appropriate for reactions to proceed Subrnit Request Answer Part A An enzyme Obinds substrates in a manner that facilitates the formation of product decreases the rate of a reaction. is always...
Help on prelab NOTE! There are FOUR (4) pages in this pre-lab! PRE-LAB WORKSHEET FOR ENZYME LAB To be completed prior to the online prelab esercise 1 ) Suppose that the diagram below represents what occurs during a chemical reaction e) Which letter points tq the prodact? print e ore , d 3) (c) Which letter points to the enzyme? (d) Which letter points to the enzyme's active site? (e) Which letter points to the enzyme's substrate? Note: Some letters...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...