Which of the following is the correct value of the KM? a. It is [substrate] at half Vmax b. It is [substrate] at Vmax c. It is half of the [enzyme] Od. It is half of the V. max
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- Which of these is not true about enzymes? A. Most of them are proteins B. Are changed at the end of the reaction C. Can only speed up the rate of the reaction D. Very specific in function E. Work better in specific mediumAssuming an excess of substrate, if the enzyme concentration is doubled in a reaction vessel, the number of substrate molecules converted to product per minute will: a. be 1/2 as much as originally b. remain the same as originally c. be twice as much as originally d. only be able to be determined experimentally e. no correct response is givenAllosteric site is the part of the enzyme where the substrate binds. * A. True B. False
- Which of the following is incorrect regarding the active site of anenzyme?a. is unique to that enzymeb. is the part of the enzyme where its substrate can fitc. can be used over and over againd. is not affected by environmental factors, such as pH andtemperatureWhich of the following best describes the relationship between an enzyme and a substrate a. stable b. causes permanent alteration to the enzyme c. results from non-complimentary bonding d. are complimentaryEnzymes are typically specific to ________. a. one substrate b. any substrate they encounter c. a handful of substrates
- For reactions to occur there needs to be what level of substrate and enzyme concentrations? Select one: a. Greater amount of substrate b. Lower amount of substrate c. Just the right amount of substrateWhich of the following statements about Competitive and noncompetitive inhibition is false? a. A noncompetitive inhibitor does not change the Km of the enzyme. b. A competitive inhibitor does not change the Vmax of the enzyme c. The noncompetitive inhibitor can bind either free enzyme or the enzyme–substrate complex. d.A competitive inhibitor decreases the apparent Km for a given substrate.An enzyme has 10 times greater affinity for substrate "A" than for substrate "B". Which of the following is true? a.) KM of A is 10 times the KM of B b.) The concentration of B is 10 times that of A c.) Vmax of A is 1/10 the Vmax of B d.) KM of A is 1/10 the KM of B e.) Vmax of A is 10 times the Vmax of B
- Which of the following statements about the Michaelis Menten constant (Km) is correct......A. can be determined by plotting the data v/[S] against 1/[S] B. A large Km indicates a low affinity between the enzyme and the substrate C. A large Km means that a large concentration of substrate is needed for the enzyme to work D. is a measure of the affinity of enzymes for proteins, minerals and vitamins E. Small Km means that a large concentration of substrate is needed for the enzyme to workThe Vmax of an enzymatic reaction can be increased by _______________. A. Increasing the enzyme concentration only. B. Increasing the substrate concentration only. C. Removing a non-competitive inhibitor. D. Removing a competitive inhibitor. E. A and C F. A, C, and DChoose the best answer The active site of an enzyme is the place where the following happens: a)The enzyme-substrate complex forms and the reaction occurs at the active site. b)The enzyme substrate complex forms here. c)The catalytic reaction happens here. d)Allosteric regulation of enzyme rate occurs here. e)All of these are correct.