6 The strategy of holding one reactant constant while the activity of a second is determined is important for defining both biological and chemical systems. Measuring enzyme-substrate activity (as in the graph below) is important in biological systems. What parameter is held constant in the graph below? 100 units of substrate emt of product fermed 10 units of substrate one unit of enzyme Lime

6 The strategy of holding one reactant constant while the activity of a second is determined is important for defining both biological and chemical systems. Measuring enzyme-substrate activity (as in the graph below) is important in biological systems. What parameter is held constant in the graph below? 100 units of substrate emt of product fermed 10 units of substrate one unit of enzyme Lime

Name: 3 6 The strategy of holding one reactant constant while the activity o
Uploaded: 2024-03-20T06:42:55.000Z
Channel: Bartleby
Description: 3 6 The strategy of holding one reactant constant while the activity of a second is determined is important fordefining both biological and chemical systems. Measuring enzyme-substrate activity (as in the graph below) isimportant in biological system

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...

See similar textbooks

Similar questions

Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
Which of the following analogies best describes the induced-fit model of enzyme-substrate binding? a hug between two people a key fitting into a lock a square peg fitting through the square bole and a round peg fitting through the round hole of a children’s toy the fitting together of two jigsaw puzzle pieces
Which of the following methods is not used by enzymes to increase the rate of reactions? a. covalent bonding with the substrate at their active site b. bringing reacting molecules into close prosimity c. orienting reactants into positions to favor transition states d. changing charges on reactants to hasten their reactivity e. increasing fit of enzyme and substrate that reduces the energy of activation
An allosteric inhibitor does which of the following? Binds to an enzyme away from the active site and changes the conformation of the active site, increasing its affinity for substrate binding Binds to the active site and blocks it from binding substrate Binds to an enzyme away from the active site and changes the conformation of the active site, decreasing its affinity for the substrate Binds directly to the active site and mimics the substrate.
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
Which of the following is not true about enzymes They increase ?G of reactions They are usually made of amino acids They lower the activation energy of chemical reactions Each one is specific to the particular substrate(s) to which it hinds.
In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.
5. Which of the following statements is/are correct regarding allosteric regulation?a) Allosteric effector controls the activity of an enzyme by irreversible binding.b) Allosteric effector binds to the regulatory sitec) Allosteric activator causes changes in the catalytic site enhancing the substrate binding.d) Allosteric inhibitor causes changes in the catalytic site decreasing the substrate binding. explain each option
1. Can the absorbance readings be used as a measure of enzyme activity atdifferent pH’s? 2. Describe an industrial application in which control of temperature and pHare critical to optimal enzymatic function.
1. There are two major categories of enzyme, inhibition, name, and describe them. 1a. Reverse inhibition can be overcome to allow the enzyme to resume is Catley activities. Describe how reversible inhibition can occur and how it can be over come.
5) Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number over an arrow (1, 2, 3, etc) represents an enzyme that catalyzes that reaction (so enzyme 2 catalyzes the conversion of B to C). Indicate all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway. please indicate each interaction in the format example: "X will inhibit enzyme 27".
3. What is the marker for the enzyme’s optimum condition?