| Explain how enzymes increare the peed of reactionExplain the most important ceason why enzymer are neCESSary in viochemicalreactions.3. Define the fullowing:a. Achive siteb. LOCK and Key modelC Induced-fit madeld. Holoenzyme8. Appenzymef. Coenzyme

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Answered: | Explain how enzymes increare the peed…

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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24. Which of the following is not part of ATP composition? A. Three phosphate groups B. Ribose C. Deoxyribose D. nitrogenous base 25. With regards to competitive inhibitors, all of the following are correct except A bind to the active site of an enzyme B competing with the substrate C. its structure is the same as the original substrate D. it binds to allosteric site and control enzyme activity
4. Based on Figure 4, at B, further increase substrate concentration produce no change in rate of reaction. Identify the term suitable at B. * C. Rate of reaction A Substrate c onc entration Figure 4 O A. Optimum temperature O B. Optimum rate of reaction O C. Denaturation D. Point of saturation B.
what is the purpose of this experiment Effect of Temperature on the Hydrolysis of Starch
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
3.Briefly explain how enzymwe descrease the activation energy of biocchemical reactions
2
What is the effect of pH on catalase activity? BIU EE E 4. Describe what you know about enzymes that explains your evidence and your claim. Use the words: pH, substrate, product, active site, 3D shape, denature, and hydrogen bonds
Endergonic reactions 000 can drive exergonic reactions have a positive AG are spontaneous have a negative AG
3. Determine how energy is produced in the protein metabolic pathway and compute for ATP production. TOPIC: Protein Metabolism/Interrelationship of the Different Catabolic Pathways
When an enzyme catalyzes a reaction: onisido stunim q a. Substrate(s) bind in the active site The b. Products bind in the active site eri c. The shape of the enzyme remains unchanged l f d. The enzyme is consumed by the reaction
STROCTURES AND FUNCIONS Use the figure to answer the following questions. 16 The most lamportan Jumetion of ude calalyslog clentcal reactions b. lorming a barrier betwoen the Inside and out side ol a call The graph below reuresets the enerty changes that occur as a chemlcal reaction progressen 17. How many calerem dnds ol momoes am ther in sart 18 How mamy dllenet nds of mnmes an hes in peteied Reactants 14 IHow many dillerent knta of monomen are theer t ac Products STRUCTURES AND FUNCTIONS Label each part of Reaction proges The dlagram below thows the lsteraction ol an eaym 6 Nhat is represented hy arrow A? 2 What is represented by arrow B7 * Is this reaction endergonic or exergonic7 Explain your answer. 9 Arrange the fallowing in order of size, trom smallest to largest: polyiner, monoiner, carbon atom, macromolecule O Hydrugen bonds a. form between lydrogen atoms in dillerent molecules. b. are strong bands c. hold water molecules to one another d. hold the two hydrogen atos together…
Create 2 illustrations of Glycolysis: (1) Name of substrates and enzymes only (2) Structure of substrates and enzyme names only

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| Explain how enzymes increare the peed of reaction Explain the most important reason why enzymer are necessary in biachemical reactions. 3. Define the fullowing 9. Achive site b. LOCK and key madel C Induced-fit madel d. Holoenzyme e. Apaenzyme