4.1 12. L-Amino-acid oxidase will catalyze reactions of L-amino acids but not of D-amino acids. Which of the following BESTdescribes the characteristic of L-amino acid oxidase?A. Group specificityB. Linkage specificityC. Reaction specificityD. Absolute specificityE. Stereochemical specificity13. What will happen to the Km and Vmax of an enzyme-substrate interaction if you slightly increase the temperature of anenzyme reaction? Assume that no enzyme denaturation occurred.A. Km increases; Vmax also increases.B. Vmax decreases; Vmax decreases.C. Km stays the same; Vmax increases.D. Km decreases; Vmax stays the same.

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L-Amino-acid oxidase will catalyze reactions of L-amino acids but not of D-amino acids. Which of the following BEST describes the characteristic of L-amino acid oxidase? A. Group specificity B. Linkage specificity C. Reaction specificity D. Absolute specificity E. Stereochemical specificity

L-Amino-acid oxidase will catalyze reactions of L-amino acids but not of D-amino acids. Which of the following BEST describes the characteristic of L-amino acid oxidase? A. Group specificity B. Linkage specificity C. Reaction specificity D. Absolute specificity E. Stereochemical specificity

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 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

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In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
1. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (DDGfold = ?) 2. An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constant Kd,S of the enzyme-substrate complex ES is 1 μM, for EC it is 10 μM. When the cofactor C is present, Kd,s’ is decreased to 0.1 μM. What is the value for the dissociation constant Kd,C’ of the enzyme-cofactor complexing the presence of substrate S? Calculate the interaction energy DDGint for cofactor and substrate binding.
3. MUTPase from ASFV (aDUT) and from swine (listed as sDUT) were studied in the absence and present of the DUTP substrate. Using the melting temperature data provided below, how does adding the substrate affect enzyme stability? Explain your choice in 25 words or less. TemperatureL°CT protein Tm by thermal denaturation (°C) aDUT 83.1 ± 0.2 SDUT 61.8 + 0.2 aDUT-DUTP-Mg SDUT-dUTP-Mg 84.5 + 0.1 62.7 + 0.2 a. The substrate makes aDUT less stable and SDUT more stable b. The substrate makes aDUT more stable and $DUT less stable c. The substrate makes both ADUT and SDUT less stable d. The substrate makes both aDUT and SDUT more stable sh (United States) D. Focus rch 7:15 80°F ENG 7/10/2 DELL F3 F4
2. Cofactors, coenzymes, and prosthetic groups are important non-protein substances that are required for enzyme function. This is a table of cofactors/coenzymes/prosthetic group we've discussed. Draw the functional portion of the cofactor/pro and explain the functional role in each reaction. a. Cofactor Name thiamine pyrophosphate (TPP) oxidized Lipoamide/lipoic acid/lipoyl-lysine Coenzyme A (CoASH) flavin adenine dinucleotide (FAD) reduced nicotinamide adenine dinucleotide (NADH + H+) oxidized nicotinamide adenine dinucleotide (NADP+) biotin Reaction Pyruvate -> acetaldehyde Pyruvate -> Acetyl CoA aKetoglutarate -> Succinyl-CoA Succinate -> Fumarate Pyruvate -> lactate 6-Phosphogluconate -> Ribulose 5- phosphate Bicarbonate + pyruvate -> oxaloacetate Structure of only the cofactor Functional or catalytic role
5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142
4. Predict the reactivity of trypsin at pH 14. C 100 50 0° 20 40° 60°C Temperature 5. What is the optimal temperature for the enzyme in graph C? Where does the enzyme in graph C most likely function? 6. Using graph C: a. Explain what happens when hypothermia sets in (when enzymes get too cold!) Reaction Rate vs Substrate Concentration ege 3 of 4 635 words English (U.S.) Text Predictions: On DII F4 近 Percent maximum activity
Penícillin is an esxample of what type of enzyme inhíbitor? A. Competitive B. Noncompetitive C. Uncompetitive D. Irreveralble What type of Inhíbition ia observed from the ahift of the Lineweaver-Burke plot ahown in the graph below where the solid line represents the uninhibited enzymatic reaction while the broken line represents the inhibited enzymatic reaction? A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhíbition D. Uncompetitive inhibition Potaszium cyanide ia a polzon which combines with cytochrome A3 to prevent binding of oxygen to the enzyme without altering the Km of the reaction with reapect to reduced cytochrome c. Which type of inhíbition does this represent? 9. A. Irreveraible inhibition B. Noncompetitive inhibition C. Competitive inhibition D. Uncompetitive inhibition Which of the following enzyme clesses catalyze reactions in which two molecules become diasociated from each other? 10. A. Kinase В. Нydrolaae C. Isomerase D. Ligase 1. Which of the…
3. Which of the following statements regarding enzymes and transition states is true? a. stabilization of the transition state must be less than stabilization of ES for catalysis to occur b. binding of substrate to an enzyme often causes strain, thus promoting transition state formation c. the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state d. formation of the transition state always assures that the reaction will proceed to product e. none of the above are true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a…
3. Enzyme specificity. To determine the specificity of substrate binding for a particular enzyme/protein, structurally related compounds may be used as potential substrates and Km values may be calculated. However, many compounds structurally related to the substrate may bind to the active site but cannot be converted to product. In these instances, the substrate analogs are used as potential competitive inhibitors of substrate binding. Low K, values indicate high affinity of the enzyme for the inhibitor, whereas high K,values indicate low binding affinity. Consider the enzyme xanthine oxidase, which catalyzes the formation of uric acid from the purine bases hypoxanthine or xanthine in humans. The Km for hypoxanthine is 15.0 μM and for xanthine it is 45.0 μM. A few compounds used as competitive inhibitors of the normal substrate hypoxanthine are listed in the table below with their K; values. Comparing the structures of hypoxanthine with the listed substrate analogs, what can you…
1. You are working on an experiment with a newly discovered enzyme. This enzyme works most efficiently at a pH of 7.70. You make 250 mL of a 150 mM phosphate buffer, pH 7.70. (pK = 6.82). a. What are the concentrations of the weak acid and conjugate base forms of this phosphate buffer when you start the experiment? b. In the process of the enzyme catalyzed reaction, 25 mM acid (H+) is produced. What is the pH of the solution after the reaction is complete? Assume no change in volume by production of the acid. 2. Case Study Questions: Normal Levels of Substances in the Arterial Blood: PH 7.40 + 0.05 pCO2 (partial pressure of carbon dioxide) 40 mm Hg pO2 (partial pressure of oxygen) Hemoglobin - O₂ saturation [HCO3-] 90-100 mm Hg 94 - 100% 24 meq / liter A. Kim is a 38 year old woman admitted to the hospital for bulimia. Her laboratory results are as follows: pH 7.48, pCO₂ in the normal range and total HCO3 higher than normal. Classify her acid- base balance as acidosis or alkalosis and…
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 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. 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 equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
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.