Why do you see a sharp decline in this graph at pHs higher and lower than 6?Effect of pH on Enzyme Activity1.210.8Enzyme 0.6Activity0.40.20+0 246pH810 12 14-Enzyme Activity

The graph shows how pH affects the activity of the enzymes. Enzyme activity is displayed on the…

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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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What is the minimum and maximum pH in which Enzyme Y will work? What is the optimal (best) pH? Y 1 2345 67891011121314 pH Rate of Enzyme Action
was 3 minutes ago + BIUA GD 田回▼ =山=一位 10. Using the following graph, explain how pH affects enzyme activity. x optimal pH 8 PH 10 Hooraul * Enzyme activly
The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (µM). 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the inhibited enzyme reaction?
Refer to the following graph when answering questions. These words may be used to fill: competitive, uncompetitive, noncompetitive, irreversible. -1 mg , μmol min-1 v-1 0.2 0.1 THA -4-2 CBA + 2 4 [S]-1, (mM-1) Word 1, The value of Km for the enzyme depicted by curve A is 2, The value of Vmax for the enzyme depicted by curve A is 3, Curve B depicts the effect of an inhibitor on the system described by curve A. This inhibitor is a inhibitor. 4, Curve C depicts the effect of a different inhibitor of the system described by curve A. This second inhibitor is a inhibitor. D
Given the active site diagram below, which best described the mechanism(s) of Active Site `NH2. SH OH - catalysis? NH -Mg²+ O Acid-Base O Acid-Base & Metal lon Covalent Catalysis Acid-Base & Covalent Catalysis O Metal lon
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."
مكالمات طوار 9:08 protein denaturation lower the energy of products 1/1 نقطة )نقاط( السؤال 1 1 An inorganic ion required for the activity of an enzyme is known as Cofactor Inhibitor Activator Coenzyme 1/0 نقطة )نقاط( السؤال 12 If Km of an enzyme to substrate A is 2x 10-5 and for „substrate B is 5x 10 4, it means
A purely competitive inhibitor of an enzyme has which of the following kinetic effects? decrease in Km increase in Vmax decrease in Vmax increase in Km Question 60 The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for KM is concentration, such as molarity It is equal to ½ of Vmax It is the substrate concentration necessary to reach ½ of Vmax
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
enzymes increase the rate of a chemical reaction by increasing the amount of activation energy needed decreasing the amount of activation energy needed decreasing the temperature increasing the temperature altering the chemical of substrates 2. which of the following is an example of quantitive data? the freshman class of the students contained 643 students, 372 males, and 271 females. the absorption peak of cobalt chloride was 510nm bromelain has optimal enzyme activity at a pH of 7 the color of cobalt chloride was pink the mass of the onion was 50 grams
an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C
Which two enzyme curves would be generated from a themophilic bacteria that lives in a strongly acid environment? Please provide a supportive statement about why you picked each of the two curves you picked. Your answer should include information from the graphs. (a) 3 5 MA A 100 7 8 20 2 40 60 Temperature (°C) I 80 ➤ (b) 1 2 3 4 PH 5 6 ➤ 9 10

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Why do you see a sharp decline in this graph at pHs higher and lower than 6? Effect of pH on Enzyme Activity 1.2 1 0.8 Enzyme 0.6 Activity 0.4 0.2 0 + T 02 4 6 pH 8 10 12 14 -Enzyme Activity