Ans 56 : c) the active site is rigid and the substrate must fit exactly.
According to the lock and key model of enzyme action , the substrate acts as a specific key that has a shape complimentary to the shape of active site of the enzyme. This ensures the specificity of the enzyme molecule as only a particular kind of substrate can bind onto it and bring about the reaction.
56. In the lock and key model of substrate binding to enzymes Pprat wnich they work...
Homework # 16: Enzymes Late assignment will be given a grade of "0. Due Date 1. An enzyme is primarily made out of a (hint what food group). catechol+ oxygen (0a) Catecholasepolyphenol 2. Looking at the equation above, the enzyme in this reaction is: 2. A. Catechol B. Oxygen C. Catecholase D. Polyphenol 3. Looking at the same equation as question 2, what is the substrate? A. Catechol B. Oxygen C. Catecholase D. Polyphenol What is the name of the...
The lock and key model and the induced fit model are two models of enzyme action explaining both the specificity and the catalytic activity of enzymes. Indicate whether cach statement is part of the lock and key model, the induced fit model, or is common to both models. Lock and key model Induced fit model Common to both models Answer Bank The substrate binds to the enzyme at the active site, forming an enzyme-substrate complex The substrate binds to the...
Please help me with this questions 11. Define active site and substrate 12. Classify enzyme 13. Difference between lock and key and induced fit model 14. Difference between, alleosteric regulation feedback inhibition, competitive and noncompetitive inhibition? 15. What the affect of high temp or PH change on enzyme 11. Define active site and substrate 12. Classify enzyme 13. Difference between lock and key and induced fit model 14. Difference between, alleosteric regulation feedback inhibition, competitive and noncompetitive inhibition? 15. What...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
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
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:...
Which amino acids in chymotrypsin are found in the active site and are participants in substrate cleavage? His, Ser, Asp His, Ser, Arg His, Ser Lys, Ser, Asp Where does cleavage of the peptide bond by chymotrypsin occur? On the C-terminal side of positively charged residues (lysine or). On the N-terminal side of aromatic residues (e.g. phonylalanine or tryprophase). On the C-terminal side of aromatic residues (e.g. phenylalanine or). All of the above When substrate concentration is much greater than...
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...
High concentrations of substrate overcome reversible inhibition by a transition-state analog because Question options: A. only the substrate has the inherent ability to bind at the active-site. B. the substrate has a greater inherent affinity for the active-site. C. transition-state analogs show noncompetitive kinetics. D. the substrate will react with the transition-state analog. E. The transition-state analog is a competitive inhibitor.