A. An increase in the substrate concentration (at constant enzyme concentration) leads to proportional decrease in the rate of the reaction. B. The optimum temperature for most enzymes operating in the human body is 37°C. C. An enzyme-substrate complex can either dissociate back into the enzyme and substrate or form a product. D. Maximal activity of many human enzymes occurs around pH 7.4.
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Biochemistry question:
Which of the following statements seen in the attached image about enzyme kinetics is FALSE?
Please help with this question. The answer choices are in the attachment.
Thank you
Step by step
Solved in 2 steps
- Please choose one of these answers A. An allosteric inhibitor appeared B. There was a dramatic change jn the pH. C. The enzyme had achieved its maximum velocity. D. The enzyme had denatured E. A large amount of the substrate had been consumed.The following graph shows enzymes activity for three different enzymes in the mamalian digestive system . PLEASE IN 10 MINSIndicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.
- The enzyme activity is: A. to The number of grams of substrate that react to form product, per mole of enzyme, per unit of time. b. The number of moles of substrate that react to form product, per gram of enzyme, per unit time. c. The number of moles of substrate that react to form product, per mole of enzyme, per unit time d. The number of grams of substrate that react to form product, per gram of enzyme, per unit of time.Which of the following is a primary function of the active site of an enzyme? a. It binds allosteric regulators of the enzyme. b. It binds noncompetitive inhibitors of the enzyme. c. It catalyzes the reaction associated with the enzyme. d. It is activated by the presence of the end product of the metabolic pathway in which the enzyme is involved. Clear my choice Question 2 Not yet answered Points out of 2.00 Flag question Question text Which of the following statement about the mass spectrometry is true? a. Large amount of protein sample is needed for mass spectrum, and thus it is very expensive. b. It is a powerful method to determine the 3-dimensional structure of proteins. c. It can be sued for protein location in a living cell. d. It can be used to measure the molecular weight of proteins. e. It can be used to determine the stability of a protein structure in solution. Clear my choice…The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.
- Which of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.Evaluate the following statements concerning enzyme kinetics. Which one of the statements is false? a. Enzyme saturation fluctuates. b. In an uninhibited enzymatic reaction system, adding an excess of substrate will increase the reaction velocity beyond Vmax. c. The Vmax of an enzyme kinetics graph represents the point at which the enzyme is saturated with substrate. d. Non-competitive inhibition of an enzymatic reaction can be overcome by adding more unaltered enzyme. e. The activation energy of a reaction can be reduced by the presence of an enzyme.Examine the graph showing the rate of reaction versus temperature for an enzyme–catalyzed reaction in a human. a. Describe what is happening to the enzyme at around 40°C. b. Explain why the line touches the x-axis at approximately 20°C and 45°C. c. Average body temperature for humans is 37°C. Suggest a reason why the temperature optimum of this enzyme is greater than 37°C.
- The following statements are either True or False. Please label accordingly. a. L-Amino reductase is an enzyme. b. Allosteric enzymes are composed of two or more protein chains. Heavy metals are examples of inhibitors. They function by binding to sulfur on cysteine amino acid residues. C. d. A reversible noncompetitive inhibitor temporarily blocks an enzyme's active site. Enzymes don't denature as easily as smaller proteins when heated or stressed due to their complex secondary and tertiary structure. e. Oxidative phosphorylation is the biochemical process by which ATP is synthesized from ADP when protons cross the inner mitochondrial membrane. f. g. DNA and RNA strands differ only in the fact that DNA forms a double helix. h. There is no secondary structure in RNA strands.Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.Which of the following will happen if the concentration of an enzyme increases for a given substrate?? a. the reaction rate increases similarly b. the rate of the reaction decreases to a point. c. there is no change in the reaction. d. the turnover number decreases at the same rate that the enzyme concentration increases. e. the reaction stops.