A molecule that is structurally Similar to the substrate for an enzyme will probably be a competitive inhibitor.
so, the answer is A
Option B is not true because
cofactor is a non-protein chemical compound that is required for an enzymes activity as catalyst, a substance that increases the rate of reaction.
Option C is not true because
It is an enzyme in an biochemical pathway which, through its responses to the presence of certain other biomolecules, regulates the pathway activity.
Option D is not true because
In noncompetitive inhibition, a molecule binds to an enzyme somewhere other than the active site.
19. A molecule that is structurally similar to the substrate for an enzyme will probably be...
18. The following kinetic scheme that shows the Inhibitor () only binding to the enzyme-substrate (ES) complex is typic of what type of enzyme inhibition? E + SEES -E + PSN ESI no reaction A) Irreversible B) Competitive C) Noncompetitive D) Uncompetitive or acetylcholinesterase 19. DIFP acts as an inhibitor of the enzyme chymotrypsin. A) Irreversible B) Competitive C) Uncompetitive D) Mixed
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work best a the substrate changes its conformation to fit the active site b. the active site changes its conformation to fit the substrate c. the active site is rigid and the substrate must fit exactly d. the substrate binds only to part of the active site In the induced-fit model of substrate binding a. 57. the substrate changes its conformation to fit the active...
Reset Help noncompetitive enzyme irreversible acetylcholinesterase competitive active site 1. A inhibitor binds to a site on the enzyme that is not the active site. 2. Insecticides and nerve gases act as irreversible inhibitors of nerve conduction. an enzyme needed for 3. A inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate. 4. Usually, an nhibitor forms a covalent bond with an amino acid side group within...
Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is: a) a competitive inhibitor b) an allosteric inhibitor c) a noncompetitive inhibitor d) a suicide inhibitor 3. Competitive inhibitors: a) bind to the active site b) bind to the enzyme-substrate complex c) bind outside the active site and decrease substrate binding d) bind outside the active site and decrease rate of catalysis.
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is:...
Compare competitive and noncompetitive inhibition Question Suppose that glycerol (CH,OHCH(OH)CH,OH) is a substrate in an enzyme-catalyzed biochemical reaction and propylene glycol (CH OHCH(OH)CHZ) is an inhibitor of the reaction. Would you expect propylene glycol to be a competitive or noncompetitive inhibitor? Why? Select the correct answer below: O It is likely that propylene glycol would be a competitive inhibitor because it easily binds to glycerol. O It is likely that propylene glycol would be a competitive inhibitor because it has...
Complete the sentences with the best answer A noncompetitive inhibitor binds to the __________________ (enzyme/enzyme-substrate complex/both) whereas an uncompetitive inhibitor binds to the ___________________ (enzyme/enzyme-substrate complex/both).
The allosteric enzyme ATCase is regulated by CTP, which binds to the T-state of ATCase. CTP is a: Select one: O A. negative regulator. B. coenzyme. C. positive regulator. D. cofactor E. competitive inhibitor.
The active site of an enzyme ____. A. is remote form the site of substrate attachment B. is converted to a product C. is the region where the reaction takes place D. increases the energy of reaction E. includes the entire enzyme In the lock-and-key model of enzyme actin, the enzyme active site is thought of as ___. A. a rigid, nonflexible shape that fits the substrate exactly B. an area of the enzyme that can adjust to fit the...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...