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- Which of the following is NOT a true statement about the diagram below? Intermediate A Intermediate B Pathway operates End-product © 2019 Parson Education ne O O O O O Substrate -Enzyme 1 Allosteric site -Enzyme 2 -Enzyme 3- Pathway shuts down Bound end-product The diagram shows a metabolic pathway Each enzyme is specific for its substrate The product of each enzyme reaction becomes a substrate for the next enzyme None of the other four answers (all are true statements) The end-product serves as a competitive inhibitor of the substrate on Enzyme 1Picture. 1: Fresh potato +H202 H2O+02 (air bubbles) Questions: 1. Why did you use buffer instead of distilled water to dilute the enzyme and the substrate? 2. What do we mean by enzyme specificity? 3. Name the substrate of peptidase, sucrase and amylase? 4. Discuss the factors affecting the rate of an enzymatic reaction, showing how each one affects the rate? 347. An enzyme-catalyzed reaction proceeds by the mechanism below: B. E+S1→ ES --2E+P E+A 3 EA EA+S4 EAS --5 EA + P E+I 6 EI EAS+I7 → EAIS -8 EIS + P K. macronutrient L. enzyme activator/cofactor M. liposome N. anaerobic process O. aerobic process E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: kı, k2, k3, k4, k5, k6, k7, and ks Rate constants (k's) for the reverse reactions are: k-1, k-3, k-4, k-6, and k-7 Write the enzyme balance for this mechanism. 4 How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the
- 8. TABLE 3.3 Catalytic Activity of a Variety of Enzymes Enzyme Nonenzymatic t,2' Turnover number? Rate enhancement 78,000,000 yr 130,000 yr 120 yr 69,000 yr 69 yr 2.9 yr 7.3 yr 7 wk 1.4 x 107 5.6 x 1014 2.1 x 1012 6.0 x 1012 1.2 x 1012 2.8 x 10" 1.9 x 10" 3.9 x 10" 1.0 x 10° 1.9 x 10 7.7 x 10 4.6 x 10 39 OMP decarboxylase Staphylococcal nuclease 95 Adenosine deaminase 370 AMP nucleosidase 60 Cylidine deaminase Phosphotriesterase Carboxypeptidase A Ketosteroid isomerase 299 2,100 578 66,000 Triosephosphate isomerase Chorismate mutase 1.9 d 4,300 7.4 hr 5 sec 50 1 x 10 Carbonic anhydrase Cyclophilin, human 23 sec 13,000 "The time that would elapse for half the reactants to be converted to product in the absence of enzyme. The number of reactions catalyzed by a single enzyme molecule per second when operating at a saturating substrate concentration. The increase in reaction rate achieved by the enzyme-catalyzed reaction over the noncatalyzed reaction. Source: A. Radzicka and R. Wolfenden,…1. define in your own words enzyme 2. explain how enzymes act on a substrate 3. explain the term catalyst 4. what is meant by optimal conditions for enzymes and what are the conditions 5. explain what catalase is: what it helps to break down and into what parts.1.The class of enzyme that catalyzes addition of a group to a double bond is? oxidoreductases lyases ligases isomerases hydrolases transferases 2. Suppose an enzyme and its substrate obey the lock and key model of enzyme catalysis. Which of the following would be true of the enzyme? the active site of the enzyme must be rigid the active site of the enzyme must be flexible only one substrate could be converted to product by the enzyme the enzyme could bind different substrates if the substrates shared a common motif somewhere in their structures the entire enzyme must be rigid 3. Which of the following enzymes is found in blood serum and is diagnostic of prostate cancer if enzyme levels are elevated? alanine aminotransferase phosphohexose isomerase lactate dehydrogenase acid phosphatase alkaline phosphatase 4. A blood test returns elevated aspartate aminotransferase levels. You suspect that the patient has suffered a heart attack. What other serum enzyme level of…
- S Savvas EasyBridge IS Savvas Realize asrealize.com/assignments/viewer/classes/61227fd32e855b44e0a77ded/assignments/96054946a5024ac29d3c30068e59b062/contents/c ming of Enzymes nzymes Drag each substrate to the enzyme with the matching active site. Enzymes 1. Changing environmental conditions, such as temperature or pH, can affect enzyme shape. How would this alter the enzyme's function? Substrates Type your answer here. acerSelect all statements that are correct. Note there might be more than 1 correct statement. Competitive inhibitors bind to an allosteric side on the enzyme Uncompetitive inhibitors bind to the substrate binding site Competitive inhibitors bind to the substrate binding site Competitive inhibitors are usually of similar size and shape than the substrate of the enzyme Non-competitive inhibitors can bind to the free enzyme but not to the enzyme-substrate complex pe here to search C 6 D 88 20°C T ENGConsider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acetyl A-ase Acetate A-ase Deacetylase A-ase B-ase ABC- Isoenzymes Protease Inhibition What is the mechanism of regulation of A-ase? Reversible Covalent modification Isoenzymes What is the mechanism of regulation of A-ase? C-ase Reversible Covalent modification Proteolytic Activation Feedback Inhibition Positive allostery
- 1. Which of the following options is a viable way to increase the Vmax of an enzymatic reaction? Increase the amount of substrate present. Increase the amount of enzyme present. Decrease the temperature of the reaction. Decrease the Km of the enzyme.1. Choose any enzyme we would find in our human body. 2. Categorize this enzyme as primary, secondary, tertiary or quarternary. 3. Name and Describe the substrate that the enzyme will work on. 4. Name and Describe if their are any cofactors/coenzymes involved in this enzyme.Determine how reaction rate (velocity) varies with substrate concentration. F3 $ 4 Substrate concentration R F Additional substrate is added when substrate concentration is low. F4 % 5 T Rate increases G 6 HOLL F5 & H 7 F6 YU J *00 8 DELL F7 K ( 9 Substrate is added when enzyme is saturated with substrate. F8 Rate decreases O Answer Bank F9 P W F10 { [ + 11 F11 } 1 F12 Additional substrate is added when substrate concentration is high but is not yet saturating. Backspace Rate is unchanged Enter Insert Print Screen Delete Home Scroll Lock End 8:26 PM 2 10/15/2023 + PgUp Pause Break PgDn