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Science

Biochemistry

enzyme

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Question

1. Can the absorbance readings be used as a measure of enzyme activity at
different pH’s?

2. Describe an industrial application in which control of temperature and pH
are critical to optimal enzymatic function.

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Use graphs to illustrate enzyme activity as a function of the following: II. a. Substrate Concentration max velocity v max Rate Substrate Concentration b. Enzyme concentration Rate Enzyme Conc. с. рH Optimum Temperature Increasod temp. results in denaturation Rate Temperature d. Temperature Optimum pH Rate Increas ing pH
How would a competitive inhibitor change the Km and the Vmax for an enzyme? Explain why a competitive inhibitor would result in these changes.
1. The enzyme you are studying uses the substrate pictured at right. An inhibitor box in the freezer contains two tubes labeled Inhibitor #1 and Inhibitor #2, along with the structures of the compounds contained within them and their respective Ki. Which one is more likely to be the non-competitive inhibitor? Inhibitor #1 K₁ = 10 μM m CH₂OH OH -0, $ OH OH Inhibitor #2 K₁ = 50 μM Briefly Justify: OH CH₂OH OH OH OH Substrate
12 Avdil DiC diLei OcL 27 dl 1.Jopm nents Enzyme Reaction Rates ts prary racker 10 20 30 40 50 2 4 6. 8. 10 Temperature (°C) pH Based on these data, this enzyme functions best at what temperature and pH? Remind O Temperature of 27°C and a pH of 4 O Temperature of 40°C and a pH of 8 Four O Temperature of 50°C and a pH of 10 Calculator O Temperature of 37°C and a pH of 6
A plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…
1. Cite five diseases that could be diagnosed with the determination of enzyme concentration. 2. Give four enzymes that are being used in medical therapy.
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.
V 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km. Estimate the Km from this graph giving the correct units. v/Vmax 1.0 0.5 0.0 0.0 vs [S] for an enzyme. Enzyme Activity vs [Substrate] :0.2 0.4 Substrate (HM): 0.6 (b) If the Vmax = 25 mmoles per minute per µmole of enzyme calculate the Keat and the specificity constant."
22
The effect of an inhibitor I on the rate of a single-substrate, enzyme-catalyzed reaction was investigated and gave the following results (See table below). a. What is the mode of action (pure competitive, mixed competitive, uncompetitive or noncompetitive) of the inhibitor? Briefly explain your answer. b. Estimate the value of Km and Vmax for uninhibited reaction.
What kind of catalysis is cysteine driving in this picture? S Los i fy R……—NHR N-H---S O. N-H H-N H-N. O Metal catalysis Covalent catalysis Base catalysis O Acid catalysis NHR²
4. Using a fluorescent model substrate, you study the kinetics of an enzyme-catalyzed reaction. You observe the below data. Write an equation describing reaction velocity (v) versus [S]. Define and provide a numerical value for any constants that you include in your equation. 16 14 12 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 [S] / mM `N' at 50 mM and observe the following In pilot experiments, you add the putative inhibitor imidazole Doesn't affect anything 1 reaction velocities: [S] = 1 mM5 µM min-1 [S] = 2 mM9 9 µM min-1 [S] = 4 mM 911 µM min-1 Is imidazole a competitive or non-competitive inhibitor? Provide a brief explanation. > 9 00 v/ µM min-