are key pof this bou.andlucleoholeNucleic Acidsgenetic infromating2. RAlA2.4. Enzymes control the rates at which the chemical reactions in a cell take place.A. Define the following terms:1. catalyst:2. enzyme:3. substrate:4. active site:5. energy of activation:B. Use all of the above terms to describe how enzymes work in a few sentences:

are key pr.- of this bou. mportani TUucleotiole Nucleic Acids 2 gene- 2. 4. Enzymes control the rates at which the chemical reactions in a cell tal A. Define the following terms: 1. catalyst: 2. enzyme: 3. substrate: origapids ertt sbobnlonsidine ne bigilpavis 2at 4. active site: 5. energy of activation: B. Use all of the above terms to describe how enzymes work in

are key pr.- of this bou. mportani TUucleotiole Nucleic Acids 2 gene- 2. 4. Enzymes control the rates at which the chemical reactions in a cell tal A. Define the following terms: 1. catalyst: 2. enzyme: 3. substrate: origapids ertt sbobnlonsidine ne bigilpavis 2at 4. active site: 5. energy of activation: B. Use all of the above terms to describe how enzymes work in

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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Fill in the blanks.: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.
2:51 Enzymes.pdf 7 of 8 Enzyme Active sites Substrates Enzyme substrate complex Enzyme is recycled Substrate modification Product C • Label the diagram on the following slide: • 1. substrates • 2. products • 3. energy of activation without enzyme • 4. energy of activation with enzyme • 5. Which has more energy in this reaction, the substrates or the products? • 6. What happens to the difference in energy during the reaction? How dees an enzyme make reaction go ster? a chemical A+B evergy Time (mim) Copyrighte T Jhe eya Son uaOLOGr TU S 22
. The first two steps of ovothiol C biosynthesis are shown below. Propose the rest of the pathway, indicating the potential involve- ment of cofactors. co- coo H NH,* Histidine Fo*, 02 reductant .coo- *H,N° coo- *H,N° COO HS* NH,* 5-Histidylcysteine sulfoxide conjugate 5-Histidylcysteine thioether conjugate Cysteine
6 The AG of a reaction is positive. Which is TRUE? The cell cannot catalyze this reaction under any conditions. O This reaction can only go forward in the cell if ATP is used. AG-AG in the cell, regardless of substrate/product concentrations. This reaction can go forward in the cell if the overall pathway has a negative AG. This reaction can go forward in the cell if the overall pathway has a positive AG. 00
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
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
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.
AA View Tell me Convert to SmartArt W- Picture Shapes - Text Box Arrange Quick d Tue Dec 6 3:13 PM ♫ Share Design Qsn 2 (a) A pathway consists of 6 enzymes (p, q, r, s, t, u) that convert substrate J to product X at a rate of 10 moles/hour. If enzyme q is increased from 5 mmoles to 35 mmoles the amount of product X increases to 20.5 moles/hour. What is the flux control coefficient for enzyme q (C¹)?
Fill in the blanks (write answers only in correct sequence). When the activation energy required is less between the reactants and the products, reaction is known as----- i. ii. The region of an enzyme where substrate molecules bind and undergo a chemical 11. reaction is known as--- 11. To produce amino acids and synthesis of NADH, cycle used is-- Metabolic cycle that takes place both in cytoplasm and mitochondria is--- Glucose 1 phosphate is converted to Glucose 6 Phosphate by the action of - Which vitamin deficiency is linked with the night blindness? Name it iv. V. vi.
A7. Consider what can be concluded about the catalytic site (substrate binding site) of phosphatase and the binding site of NaF from the type of inhibition shown by NaF for phosphatase and illustrate it schematically. The inhibition typre is pure noncompetitive inhibition.
10 answer this question, please reference ine Problem Solving video: Michaens-Menten Equations and Lineweaver-Burk Plots. Double-reciprocal, or Lineweaver-Burk, plots can reveal the type of enzyme inhibition exhibited by an inhibitor. Competitive inhibitors increase the KM without affecting the Vmax. Noncompetitive inhibitors decrease the Vmax without affecting the KM. Uncompetitive inhibitors decrease both the KM and Vmax 1 -> competitive noncompetitive uncompetitive cannot be determined + Inhibitor No inhibitor. 1 [S] Based on the Lineweaver-Burk plot, what type of enzyme inhibition is exhibited by the inhibitor?
MAKE A GRAPH FOR ME ON GRAPH PAPER CALL IT ENZYMES VS RATE OF REACTION USING TABLE BELOW GRAPH paper INSERTED BELOW rules: data points must be an x or circled dot, must be on grid paper , the independant variable on the x axis and dependant variable on the y axis, must include titles Regarding the data points: - H2O2 + MnO2 Control #1: (Control #1, 5)- H2O2 + sand control #2: (Control #2, 0)- Plant versus Animal Liver Catalase: (Liver, 4)- Potato: Plant vs. Animal Catalase: (Potato, 3)- Substance Enzyme Concentration (Used Liver): (Liver Used, 4)- Substance Enzyme Concentration (Used H2O2): (Used H2O2, 1) - Boiling Water Bath Temperature: (Boiling Water Bath, 5)- Ice Water Bath Temperature: (Ice Water Bath, 2)- HCl, or pH 3: (H 3, 4)- NaOH at pH 12: (pH 12, 2)- pH 7 (H2O): (assuming average of pH readings; pH 7, not specified) The following explains how to display the graph: Title: Factors versus Enzyme Activity Rate - Labels on X- and Y-axes: Factors and Rate of Enzyme…