8. Which of the following enzyme types catalyzes the formation of a single bond between two substrates? A Ligase B. Oxidoreductase C. Isomerase D. Hydrolase active site 9. Enzymes undergo n decrease in catalytic efficiency in the presence of excess temperature but can regain this efficienc y once temperature returns to normal: this suggests that temperature does not disrupt which of the following aspects of enzyme structure? A. Peptide bonds B. Van der Waal's forces C. Hydrophobic interactions D. Hydrogen bonds 10. Local conditions can affect the specificity of an enzyme for its substrate, and thus the enzymes catalytic ability: which of th alterations would most likely not affect an enzyme in this manner? A. Increased temperature B. Increased concentration of H+ C. Increased substrate concentration D. Increased concentration of salts 11. Enzymes catalyze biochemical reactions by altering which of the following quantities associated with the reaction? A. The change in Gibb's free energy Delta G B. The equilibrium constant k_(eq) C. The enthalpy of formation Delta H D. The activation energy E_(a) 12. Potassium cyanide is a poison which combines with cytochrome to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c .Which type of inhibition does this represent? A. Noncompetitive inhibition B. Reversible inhibition C. Competitive inhibition 13. In the first step of glycolysis hexokinase produces glucose-6-phosphate G-6-P itself can also bind to hexokinase at the active site , blocking access to ATP. This is an example of: A. Allosteric inhibition B. Feedback inhibition C. Uncompetitive inhibition

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8. Which of the following enzyme types catalyzes the formation of a single bond between two substrates? A Ligase B. Oxidoreductase C. Isomerase D. Hydrolase active site 9. Enzymes undergo n decrease in catalytic efficiency in the presence of excess temperature but can regain this efficienc y once temperature returns to normal: this suggests that temperature does not disrupt which of the following aspects of enzyme structure? A. Peptide bonds B. Van der Waal's forces C. Hydrophobic interactions D. Hydrogen bonds 10. Local conditions can affect the specificity of an enzyme for its substrate, and thus the enzymes catalytic ability: which of th alterations would most likely not affect an enzyme in this manner? A. Increased temperature B. Increased concentration of H+ C. Increased substrate concentration D. Increased concentration of salts 11. Enzymes catalyze biochemical reactions by altering which of the following quantities associated with the reaction? A. The change in Gibb's free energy Delta G B. The equilibrium constant k_(eq) C. The enthalpy of formation Delta H D. The activation energy E_(a) 12. Potassium cyanide is a poison which combines with cytochrome to prevent binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome c .Which type of inhibition does this represent? A. Noncompetitive inhibition B. Reversible inhibition C. Competitive inhibition 13. In the first step of glycolysis hexokinase produces glucose-6-phosphate G-6-P itself can also bind to hexokinase at the active site , blocking access to ATP. This is an example of: A. Allosteric inhibition B. Feedback inhibition C. Uncompetitive inhibition

Answer 1

8. A. LigaseLigase enzymes catalyze the formation of a single bond between two substrates. They are involved in the joining of two molecules, typically with the consumption of ATP.9. D. Hydrogen bondsIncreased temperature can disrupt hydrogen bonds in the enzyme, leading to a decrease in catalytic efficiency. However, once the temperature returns to normal, these hydrogen bonds can reform, allowing the enzyme to regain its efficiency.10. C. Increased substrate concentrationIncreasing the substrate concentration can affect the enzyme's catalytic ability by increasing the rate of reaction. However, it does not alter the specificity of the enzyme for its substrate.11. D. The activation energy

Enzymes catalyze biochemical reactions by lowering the activation energy required for the reaction to occur, thereby increasing the rate of the reaction.12. A. Noncompetitive inhibitionPotassium cyanide combines with cytochrome c to prevent the binding of oxygen to the enzyme without altering the Km of the reaction with respect to reduced cytochrome C. This represents noncompetitive inhibition, where the inhibitor binds to a site other than the active site of the enzyme.13. B. Feedback inhibitionIn the first step of glycolysis, glucose-6-phosphate (G-6-P) can bind to hexokinase at the active site, blocking access to ATP. This is an example of feedback inhibition, where the end product of a metabolic pathway inhibits an enzyme involved in its own synthesis.

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