Past Years Questions Chpater 6

Size: px
Start display at page:

Download "Past Years Questions Chpater 6"

Transcription

1 Past Years Questions Chpater 6 **************************************** 1) Which of the following about enzymes is Incorrect? A) Most enzymes are proteins. B) Enzymes are biological catalysts. C) Enzymes increase the rate of reactions by lowering the free energy of activation. D) Enzymes alter the equilibrium constant of the reaction they catalyze. Solution: the answer c is correct because the free energy of activation is the same as activation energy (same meaning). *************************************************** 2) Which of the following statements is NOT CORRECT for an enzyme-catalyzed reaction? A) The substrate binds to the enzyme B) both the substrate and product molecules are bound to the enzyme molecule. C) the product is formed at the enzyme molecule then released D) product-enzyme complex is formed during the reaction. Note: the product molecules aren t bound to the enzyme, it is formed at the enzyme then released. *************************************************** 3) To catalyze a reaction an enzyme must: A) not bind to its substrate. B) increase the activation energy of the reaction. C) increase the rate of the reaction. 4) The rate constant for the dissociation of the ES complex to free enzyme and substrate is: A) k 1 B) k 2 Page 1 of 11

2 C) kcat D) k-1 5) At the beginning of an enzyme-catalyzed reaction the is negligible. A) Formation of ES B) Formation of P C) Conversion of ES to E + S D) Disappearance of ES 6) The turnover numbers of the following enzymes are: Chymortypsin, 1.9x10 2 sec -1 Carbonic anhydrase, 1x10 6 sec -1 Acetylcholinesterase, 1.4x10 4 sec -1 Lysozyme 0.5 sec -1. now The most efficient enzyme of these is: A) Chymotrypsin B) Acetylcholinesterase C) Lysozyme D) Carbonic anhydrase. Solution: The most efficient enzyme is the highest turnover number. 7) In a Lineweaver-Burk plot, one plots 1/ [S] on the X-axis versus on the Y-axis: A) [S] B) 1/V C) 1/V max D) 1/ Km Page 2 of 11

3 8) To catalyze a reaction an enzyme must : A) increase the equilibrium constant of the reaction. B) bind to its substrate. C) increase the activation energy of the reaction. D) decrease the rate of the reaction. 9) The turnover number of an enzyme, a quantity equal to which of the following constants? A) k 1 B) k 2 C) k cat D) k -1 10) The rate constant for the formation of E + S from the enzymesubstrate complex is: A) k 1 B) k 2 C) k cat D) k -1 11) Which of the following relations is correct when [S] is much greater than K m? A) the reaction is zero order. B) V initial is proportional to [S]. C) V initial = ½ V max. D) V initial = V max. note: when the reactants are so high the reaction is always zero order. Page 3 of 11

4 12) Increasing temperature (T) has this effect on enzyme reactions: A) Temperature has little effect on enzyme reactions. B) Increasing T increases the rate of enzyme reactions over wide temperature ranges. C) Increasing T increases the rate of enzyme reactions until the heat denatures the enzyme. D) Enzymes always work fastest at the normal T of the organism in which they are found. 13) Given the rate law, rate = k[a][b], the overall reaction order is A) Zero B) One C) Two D) can t be determined. solution: the overall reaction order = sum of the all exponents of the reactants concentrations mean [A] 1 [B] 1 = +1+1= +2 14) Which of the following are related for a given enzyme? A) V max, K m, and percentage of alpha helix. B) V max, k cat, and percentage of ßeta sheet. C) V max, k cat, and turnover number. D) V max, K m, and molecular weight. 15) In a Lineweaver-Burk plot, the y intercept equals: A) [S] B) K m C) 1/V max D) 1/K m Page 4 of 11

5 16) Which of the following statements about enzymes is NOT CORRECT? A) Most enzymes are globular proteins. B) Enzymes are biological catalysts. C) Enzymes decrease the rate of the reactions they catalyze. D) Enzymes do not affect the equilibrium constant of the reaction they catalyze. 17) An enzyme-catalyzed reaction has zero order at : A) [S] = 2Km B) V max C) [S] << Km D) [S] = Km note: the zero order reaction is characterized by V max and high concentration of substrate ((more more than K m )). 18) To catalyze a reaction an enzyme must: A) not alter the equilibrium constant of the reaction. B) not bind to its substrate. C) decrease the activation energy of the reaction. D) decrease the rate of the reaction. 19) The Michaelis constant (K m ) of an enzyme catalyzed a single substrate reaction is: A) The equilibrium constant for the reaction between substrate and enzyme. B) It is a rate constant for the forward reaction. C) An index of the catalytic power of the enzyme. D) substrate concentration giving ½ maximum reaction velocity. Page 5 of 11

6 20) In the induced-fit model of substrate binding to enzymes : A) the substrate changes its conformation to fit the active site B) the active site changes its conformation to fit the substrate C) there is a conformational change in the enzyme when the substrate binds. D) there is aggregation of several enzyme molecules when the substrate binds. 21) A Lineweaver-Burk plot is useful in the analysis of enzymatic reactions because: A) it is easier to see whether points deviate from a straight line than from a curve. B) it is not affected by the presence of inhibitors C) it can be used whether or not the enzyme displays Michaelis- Menten kinetics D) It is faster in establishing a conclusion about the reaction. 22) The K m of hexokinase for glucose = 0.15 mm and for fructose K m = 1.5 mm, Which is the preferred substrate? A) Glucose. B) Fructose. C) Neither substrate is preferred over the other. D) You cannot tell from the data given. Solution: the Lower Km is the higher affinity and preferred subdstrate. 23) The rate constant for the decomposition of the enzyme-substrate complex into enzyme and product is: A) k1 B) k-2 C) k2 Page 6 of 11

7 24) The Michaelis constant (K m ) of an enzyme-catalyzed reaction represents the dissociation constant of ES when: A) k-1 = k2 B) k-1 = k1 C) k-1 >> k2 D) k1 >>k2 solution: because K m = (k -1 + k 2 ) / k 1 so when K -1 >>> k 2 The k 2 become negligible and the K m = k -1 /k 1 (k-1 = dissociation constant of ES). 25) At which of the following substrate concentration values will the reaction velocity (V) be equal to ½ of V max? A) [S] = K m B) [S] = 10 K m C) [S] = ½ K m D) [S] = 2 K m 26) The order of enzymatic reaction at a substrate concentration much smaller than K m is: A) Zero-order. B) First-order. C) Second-order. D) Third-order. 27) In the double reciprocal plot of data from enzyme-catalyzed reactions the slope equals: A) 1/V max B) -1/K m C) K m /V max D) V max /K m Page 7 of 11

8 28) Which of the following statements about most enzymes is INCORRECT? A) Are proteins. B) Are highly specific. C) Increase the rate of reaction. D) Increase the activation energy. 29) The reason to rewrite the Michaelis-Menten equation (such as the Lineweaver-Burk plot) is to : A) visualize reactions better. B) form enzyme kinetic data as a hyperbolic curve. C) calculate catalytic proficiency. D) calculate V max and K m. 30) The Michaelis constant, K m, is equal to the. A) maximum velocity that any given enzyme reaction can achieve B) substrate concentration which gives the best enzyme assay for an enzyme reaction C) substrate concentration when the rate is equal to half its maximal value. D) maximum velocity divided by two. 31) Which enzyme below is fastest? A) kinase, kcat = 10 3 B) papain, kcat = 10 C) carboxypeptidase, kcat = 10 2 D) catalase, kcat = 10 7 Solution: The highest K cat (turnover number) is the fastest enzyme. END OF CHAPTER 6 Page 8 of 11

9 Past Years Questions Chapter 7 **************************************** 1) Allosteric effectors: A) induce a conformational change in the protein to alter its activity. B) convert the enzyme either to the R or the T state C) can be very different in structure than the substrates of the enzyme D) All of the above are correct. 2) The reactive center of coenzyme A is : A) ADP. B) pantothenate. C) beta-alanine. D) 2-mercaptoethylamine. 3) Allosteric enzymes have all the following properties EXCEPT A) can be affected by feedback inhibition. B) can be activated and inhibited by effectors. C) can be described by Michaelis-Menten kinetics. D) their kinetics follow a sigmoidal curve. 4) Which of the following is true about the mechanism of chymotrypsin action? A) The two amino acid residues Ser195, and His57,are involved. B) The oxygen atom of Ser195 acts as a nucleophile. C) Water acts as a nucleophile. D) All of these are correct. Page 9 of 11

10 5) Which of the following statements is False about effects of binding inhibitors with the concerted model for allosteric behavior? A) There is an increase in the number of T-conformers. B) An inhibitor inhibits association of S and A with R. C) An inhibitor decreases cooperativity of substrate saturation curve. D) An inhibitor raises the apparent value of L. 6) Which of the following statements is NOT CORRECT for glycogen phosphorylase? A) the phosphorylated form of the T state is more active than the phosphorylated form of the R state. B) its activity can be affected by allosteric regulation. C) glucose-6-phosphate is an inhibitor of the enzyme. D) its phosphorylation requires the enzyme phosphoprylas kinase. 7) Which of the following statements is CORRECT about the enzyme carboxypeptidase A? A) its action involves metal-ion catalysis. B) its action requires Mg (II) ion. C) its activated by phosphorylation. D) it catalyzes the hydrolysis of amylase. 8) Which is incorrect : - while changing the K system, the V max change. 9) Which is incorrect : A) L initially is low. B) T initially is high. Page 10 of 11

11 10) Which is correct : - Glycogen phosphorylase is under allosteric modification. 11) The 1 st step to prepare chymotripsin is : - cleavage by trypsin. 12) The coenzyme that remove one Carbon is : -Tetrahydrofolate. 13)Which is correct about Co-enzyme A : A) It contains ATP B) The reaction is endorgonic. C) Contain pantothenic vitamin. 14) Which of the following is incorrect about ATcase? A) inhibtiory by CTP. B) inhibitory by ATP. END OF CHAPTER 7 Good Luck in your exam ^^ Your brother : Ammar Madkhana Page 11 of 11

Enzymes: The Catalysts of Life

Enzymes: The Catalysts of Life Chapter 6 Enzymes: The Catalysts of Life Lectures by Kathleen Fitzpatrick Simon Fraser University Activation Energy and the Metastable State Many thermodynamically feasible reactions in a cell that could

More information

FIRST BIOCHEMISTRY EXAM Tuesday 25/10/ MCQs. Location : 102, 105, 106, 301, 302

FIRST BIOCHEMISTRY EXAM Tuesday 25/10/ MCQs. Location : 102, 105, 106, 301, 302 FIRST BIOCHEMISTRY EXAM Tuesday 25/10/2016 10-11 40 MCQs. Location : 102, 105, 106, 301, 302 The Behavior of Proteins: Enzymes, Mechanisms, and Control General theory of enzyme action, by Leonor Michaelis

More information

Biochemistry Department. Level 1 Lecture No : 3 Date : 1 / 10 / Enzymes kinetics

Biochemistry Department. Level 1 Lecture No : 3 Date : 1 / 10 / Enzymes kinetics Biochemistry Department Level 1 Lecture No : 3 Date : 1 / 10 / 2017 Enzymes kinetics 1 Intended Learning Outcomes By the end of this lecture, the student will be able to: 1.Understand what is meant by

More information

Biochem sheet (5) done by: razan krishan corrected by: Shatha Khtoum DATE :4/10/2016

Biochem sheet (5) done by: razan krishan corrected by: Shatha Khtoum DATE :4/10/2016 Biochem sheet (5) done by: razan krishan corrected by: Shatha Khtoum DATE :4/10/2016 Note about the last lecture: you must know the classification of enzyme Sequentially. * We know that a substrate binds

More information

The MOLECULES of LIFE

The MOLECULES of LIFE The MOLECULES of LIFE Physical and Chemical Principles Solutions Manual Prepared by James Fraser and Samuel Leachman Chapter 16 Principles of Enzyme Catalysis Problems True/False and Multiple Choice 1.

More information

Chapter 11: Enzyme Catalysis

Chapter 11: Enzyme Catalysis Chapter 11: Enzyme Catalysis Matching A) high B) deprotonated C) protonated D) least resistance E) motion F) rate-determining G) leaving group H) short peptides I) amino acid J) low K) coenzymes L) concerted

More information

Tala Saleh. Ahmad Attari. Mamoun Ahram

Tala Saleh. Ahmad Attari. Mamoun Ahram 23 Tala Saleh Ahmad Attari Minna Mushtaha Mamoun Ahram In the previous lecture, we discussed the mechanisms of regulating enzymes through inhibitors. Now, we will start this lecture by discussing regulation

More information

Enzymes. Enzyme. Aim: understanding the basic concepts of enzyme catalysis and enzyme kinetics

Enzymes. Enzyme. Aim: understanding the basic concepts of enzyme catalysis and enzyme kinetics Enzymes Substrate Enzyme Product Aim: understanding the basic concepts of enzyme catalysis and enzyme kinetics Enzymes are efficient Enzyme Reaction Uncatalysed (k uncat s -1 ) Catalysed (k cat s -1 )

More information

ANSC 689 PHYSIOLOGICAL CHEMISTRY OF LIVESTOCK SPECIDS. Enzyme Kinetics and Control Reactions

ANSC 689 PHYSIOLOGICAL CHEMISTRY OF LIVESTOCK SPECIDS. Enzyme Kinetics and Control Reactions Handout Enzyme Kinetics and Control Reactions ANSC 689 PHYSIOLOGICAL CHEMISTRY OF LIVESTOCK SPECIDS Enzyme Kinetics and Control Reactions I. Kinetics A. Reaction rates 1. First order (reaction rate is

More information

Six Types of Enzyme Catalysts

Six Types of Enzyme Catalysts Six Types of Enzyme Catalysts Although a huge number of reactions occur in living systems, these reactions fall into only half a dozen types. The reactions are: 1. Oxidation and reduction. Enzymes that

More information

REGULATION OF ENZYME ACTIVITY. Medical Biochemistry, Lecture 25

REGULATION OF ENZYME ACTIVITY. Medical Biochemistry, Lecture 25 REGULATION OF ENZYME ACTIVITY Medical Biochemistry, Lecture 25 Lecture 25, Outline General properties of enzyme regulation Regulation of enzyme concentrations Allosteric enzymes and feedback inhibition

More information

Enzymes. Enzymes : are protein catalysts that increase the rate of reactions without being changed in the overall process.

Enzymes. Enzymes : are protein catalysts that increase the rate of reactions without being changed in the overall process. Enzymes Enzymes Enzymes : are protein catalysts that increase the rate of reactions without being changed in the overall process. All reactions in the body are mediated by enzymes A + B E C A, B: substrate

More information

GENERAL THOUGHTS ON REGULATION. Lecture 16: Enzymes & Kinetics IV Regulation and Allostery REGULATION IS KEY TO VIABILITY

GENERAL THOUGHTS ON REGULATION. Lecture 16: Enzymes & Kinetics IV Regulation and Allostery REGULATION IS KEY TO VIABILITY GENERAL THOUGHTS ON REGULATION Lecture 16: Enzymes & Kinetics IV Regulation and Allostery Margaret A. Daugherty Fall 2004 1). Enzymes slow down as product accumulates 2). Availability of substrates determines

More information

Student Biochemistry I Homework III Due 10/13/04 64 points total (48 points based on text; 16 points for Swiss-PDB viewer exercise)

Student Biochemistry I Homework III Due 10/13/04 64 points total (48 points based on text; 16 points for Swiss-PDB viewer exercise) Biochemistry I Homework III Due 10/13/04 64 points total (48 points based on text; 16 points for Swiss-PDB viewer exercise) 1). 20 points total T or F; if false, provide a brief rationale as to why. Only

More information

Mechanisms of Enzymes

Mechanisms of Enzymes Mechanisms of Enzymes Presented by Dr. Mohammad Saadeh The requirements for the Pharmaceutical Biochemistry I Philadelphia University Faculty of pharmacy How enzymes work * Chemical reactions have an energy

More information

Nafith Abu Tarboush DDS, MSc, PhD

Nafith Abu Tarboush DDS, MSc, PhD Nafith Abu Tarboush DDS, MSc, PhD natarboush@ju.edu.jo www.facebook.com/natarboush Biochemical Kinetics: the science that studies rates of chemical reactions An example is the reaction (A P), The velocity,

More information

Name: Student Number

Name: Student Number UNIVERSITY OF GUELPH CHEM 454 ENZYMOLOGY Winter 2003 Quiz #1: February 13, 2003, 11:30 13:00 Instructor: Prof R. Merrill Instructions: Time allowed = 80 minutes. Total marks = 34. This quiz represents

More information

Margaret A. Daugherty Fall 2003

Margaret A. Daugherty Fall 2003 Enzymes & Kinetics IV Regulation and Allostery ENZYME-SUBSTRATE INTERACTIONS THE LOCK & KEY MODEL Margaret A. Daugherty Fall 2003 A perfect match between enzyme and substrate can explain enzyme specificity

More information

Figure 1 Original Advantages of biological reactions being catalyzed by enzymes:

Figure 1 Original Advantages of biological reactions being catalyzed by enzymes: Enzyme basic concepts, Enzyme Regulation I III Carmen Sato Bigbee, Ph.D. Objectives: 1) To understand the bases of enzyme catalysis and the mechanisms of enzyme regulation. 2) To understand the role of

More information

BIOCHEMISTRY I HOMEWORK III DUE 10/15/03 66 points total + 2 bonus points = 68 points possible Swiss-PDB Viewer Exercise Attached

BIOCHEMISTRY I HOMEWORK III DUE 10/15/03 66 points total + 2 bonus points = 68 points possible Swiss-PDB Viewer Exercise Attached BIOCHEMISTRY I HOMEWORK III DUE 10/15/03 66 points total + 2 bonus points = 68 points possible Swiss-PDB Viewer Exercise Attached 1). 20 points total T or F (2 points each; if false, briefly state why

More information

Chapter 10. Regulatory Strategy

Chapter 10. Regulatory Strategy Chapter 10 Regulatory Strategy Regulation of enzymatic activity: 1. Allosteric Control. Allosteric proteins have a regulatory site(s) and multiple functional sites Activity of proteins is regulated by

More information

Lecture 6: Allosteric regulation of enzymes

Lecture 6: Allosteric regulation of enzymes Chem*3560 Lecture 6: Allosteric regulation of enzymes Metabolic pathways do not run on a continuous basis, but are regulated according to need Catabolic pathways run if there is demand for ATP; for example

More information

4-The effect of sucrose concentration on the rate of reaction catalyzed by β-fructofuranosidase enzyme.

4-The effect of sucrose concentration on the rate of reaction catalyzed by β-fructofuranosidase enzyme. Kinetics analysis of β-fructofuranosidase enzyme 4-The effect of sucrose concentration on the rate of reaction catalyzed by β-fructofuranosidase enzyme. One of the important parameter affecting the rate

More information

Dr. Nafeth Abu-Tarbou sh Introduction to Biochemist ry 15/08/2014 Sec 1,2, 3 Sheet #21 P a g e 1 Written by Baha Aldeen Alshraideh

Dr. Nafeth Abu-Tarbou sh Introduction to Biochemist ry 15/08/2014 Sec 1,2, 3 Sheet #21 P a g e 1 Written by Baha Aldeen Alshraideh P a g e 1 Enzyme Kinetics Vmax: The Maximal rate - The rate of reaction when the enzyme is saturated with substrate. -You can calculate it by the following equation: Vmax = k2 [E] T [E]T :Total enzyme

More information

1. Measurement of the rate constants for simple enzymatic reaction obeying Michaelis- Menten kinetics gave the following results: =3x10-5 = 30μM

1. Measurement of the rate constants for simple enzymatic reaction obeying Michaelis- Menten kinetics gave the following results: =3x10-5 = 30μM 1. Measurement of the rate constants for simple enzymatic reaction obeying Michaelis- Menten kinetics gave the following results: k 1 = 2 x 10 8 M -1 s -1, k 2 = 1 x 10 3 s -1, k 3 = 5 x 10 3 s -1 a) What

More information

v o = V max [S] rate = kt[s] e V max = k cat E t ΔG = -RT lnk eq K m + [S]

v o = V max [S] rate = kt[s] e V max = k cat E t ΔG = -RT lnk eq K m + [S] Exam 3 Spring 2017 Dr. Stone 8:00 Name There are 100 possible points on this exam. -ΔG / RT v o = V max [S] rate = kt[s] e V max = k cat E t ΔG = -RT lnk eq K m + [S] h rate forward = k forward [reactants]

More information

CHEM 527 SECOND EXAM FALL 2006

CHEM 527 SECOND EXAM FALL 2006 CEM 527 SECD EXAM FALL 2006 YUR AME: TES: 1. Where appropriate please show work if in doubt show it anyway. 2. Pace yourself you may want to do the easier questions first. 3. Please note the point value

More information

Anas Kishawi. Zaid Emad. Nafez abu tarboush

Anas Kishawi. Zaid Emad. Nafez abu tarboush 24 Anas Kishawi Zaid Emad Nafez abu tarboush Hello everybody, this sheet is done according to Dr. Nafith s lecture so try to use his slides for the best understanding, and good luck. WAYS OF CHANGING THE

More information

1. For the following reaction, at equilibrium [S] = 5 mm, [P] = 0.5 mm, and k f = 10 s -1. k f

1. For the following reaction, at equilibrium [S] = 5 mm, [P] = 0.5 mm, and k f = 10 s -1. k f 1. For the following reaction, at equilibrium [S] = 5 mm, [P] = 0.5 mm, and k f = 10 s -1. S k f k r P a) Calculate K eq (the equilibrium constant) and k r. b) A catalyst increases k f by a factor of 10

More information

االمتحان النهائي لعام 1122

االمتحان النهائي لعام 1122 االمتحان النهائي لعام 1122 Amino Acids : 1- which of the following amino acid is unlikely to be found in an alpha-helix due to its cyclic structure : -phenylalanine -tryptophan -proline -lysine 2- : assuming

More information

Fall 2005: CH395G - Exam 2 - Multiple Choice (2 pts each)

Fall 2005: CH395G - Exam 2 - Multiple Choice (2 pts each) Fall 2005: CH395G - Exam 2 - Multiple Choice (2 pts each) These constants may be helpful in some of your calculations: Avogadro s number = 6.02 x 10 23 molecules/mole; Gas constant (R) = 8.3145 x 10-3

More information

بسم هللا الرحمن الرحيم

بسم هللا الرحمن الرحيم بسم هللا الرحمن الرحيم Q1: the overall folding of a single protein subunit is called : -tertiary structure -primary structure -secondary structure -quaternary structure -all of the above Q2 : disulfide

More information

Human Biochemistry. Enzymes

Human Biochemistry. Enzymes Human Biochemistry Enzymes Characteristics of Enzymes Enzymes are proteins which catalyze biological chemical reactions In enzymatic reactions, the molecules at the beginning of the process are called

More information

Enzymes. Enzymes accelerate chemical reactions as the engine accelerates this drag race.

Enzymes. Enzymes accelerate chemical reactions as the engine accelerates this drag race. Chapter 30 Enzymes Enzymes accelerate chemical reactions as the engine accelerates this drag race. Introduction to General, Organic, and Biochemistry, 10e John Wiley & Sons, Inc Morris Hein, Scott Pattison,

More information

ENZYMES: CLASSIFICATION, STRUCTURE

ENZYMES: CLASSIFICATION, STRUCTURE ENZYMES: CLASSIFICATION, STRUCTURE Enzymes - catalysts of biological reactions Accelerate reactions by a millions fold Common features for enzymes and inorganic catalysts: 1. Catalyze only thermodynamically

More information

Metabolic Biochemistry / BIBC 102 Midterm Exam / Spring 2011

Metabolic Biochemistry / BIBC 102 Midterm Exam / Spring 2011 Metabolic Biochemistry / BIBC 102 Midterm Exam / Spring 2011 I. (25 points) Fill in all of the enzyme catalyzed reactions which convert glycogen to lactate. Draw the correct structure for each intermediate

More information

A cell s metabolism is all the organism s chemical reactions. Metabolism manages the material and energy resources of the cell.

A cell s metabolism is all the organism s chemical reactions. Metabolism manages the material and energy resources of the cell. Enzymes Metabolism Metabolism A cell s metabolism is all the organism s chemical reactions. Metabolism manages the material and energy resources of the cell. Energy is the capacity to do work. Metabolism

More information

Enzymes Part III: regulation II. Dr. Mamoun Ahram Summer, 2017

Enzymes Part III: regulation II. Dr. Mamoun Ahram Summer, 2017 Enzymes Part III: regulation II Dr. Mamoun Ahram Summer, 2017 Advantage This is a major mechanism for rapid and transient regulation of enzyme activity. A most common mechanism is enzyme phosphorylation

More information

UNIVERSITY OF GUELPH CHEM 4540 ENZYMOLOGY Winter 2005 Quiz #2: March 24, 2005, 11:30 12:50 Instructor: Prof R. Merrill ANSWERS

UNIVERSITY OF GUELPH CHEM 4540 ENZYMOLOGY Winter 2005 Quiz #2: March 24, 2005, 11:30 12:50 Instructor: Prof R. Merrill ANSWERS UNIVERSITY F GUELPH CHEM 4540 ENZYMLGY Winter 2005 Quiz #2: March 24, 2005, 11:30 12:50 Instructor: Prof R. Merrill ANSWERS Instructions: Time allowed = 80 minutes. Total marks = 30. This quiz represents

More information

kcat, but isozyme M (in muscle) has a Km of 5 um and isozyme L (in liver) has a Km of 20 um. Answer

kcat, but isozyme M (in muscle) has a Km of 5 um and isozyme L (in liver) has a Km of 20 um. Answer Name ENZYMES and KINETICS (10 points this page) A substrate S is converted into product P. When an enzyme is added to the reaction, the activation energy is lowered. Use single sentence answers for the

More information

Chapter 11 Enzymes and Metabolic Pathways

Chapter 11 Enzymes and Metabolic Pathways Chapter 11 Enzymes and Metabolic Pathways 11.1. Metabolism Metabolism comes from the Greek metabole, meaning "change". It is an emergent property of life. It includes all the chemical processes needed

More information

رمضان كريم. 1Page كالشمس للدنيا

رمضان كريم. 1Page كالشمس للدنيا Slide # 17 ( michaelis- menten approach) : Most enzymes adopt a certain behavior that involves first order + zero order in their reactions When the German scientist studied the enzyme kinetics, he put

More information

An Introduction to Enzyme and Coenzyme Chemistry, 2nd Ed. T. D. H. Bugg, Blackwell Science, Oxford, 2004

An Introduction to Enzyme and Coenzyme Chemistry, 2nd Ed. T. D. H. Bugg, Blackwell Science, Oxford, 2004 Combinatorial synthesis of linchpin β-turn mimic 1 2 DCC, BT 1 2 n -tbu 1 n -tbu 1) 2 FMC DCC, BT 2) piperidine 1 2 2 n -tbu 3 DCC, BT 1 2 n -tbu 3 1) Ph 3 P 2) cyclization 3) CF 3 C 2 2 1 n 3 2 Evaluated

More information

Enzymes. Gibbs Free Energy of Reaction. Parameters affecting Enzyme Catalysis. Enzyme Commission Number

Enzymes. Gibbs Free Energy of Reaction. Parameters affecting Enzyme Catalysis. Enzyme Commission Number SCBC203 Enzymes Jirundon Yuvaniyama, Ph.D. Department of Biochemistry Faculty of Science Mahidol University Gibbs Free Energy of Reaction Free Energy A B + H 2 O A OH + B H Activation Energy Amount of

More information

Biology 2180 Laboratory #3. Enzyme Kinetics and Quantitative Analysis

Biology 2180 Laboratory #3. Enzyme Kinetics and Quantitative Analysis Biology 2180 Laboratory #3 Name Introduction Enzyme Kinetics and Quantitative Analysis Catalysts are agents that speed up chemical processes and the catalysts produced by living cells are called enzymes.

More information

CHM 341 C: Biochemistry I. Test 2: October 24, 2014

CHM 341 C: Biochemistry I. Test 2: October 24, 2014 CHM 341 C: Biochemistry I Test 2: ctober 24, 2014 This test consists of 14 questions worth points. Make sure that you read the entire question and answer each question clearly and completely. To receive

More information

Page 8 the draw of Histidine There is a Beta-carbon missed; there should be "CH2" attached to the alpha-carbon.

Page 8 the draw of Histidine There is a Beta-carbon missed; there should be CH2 attached to the alpha-carbon. Sec 1,2,3 : Sheet #1 Page 4 Paragraph 3 The correction is: "(has a plane of symmetry)" The wrong sentence was: "(does not have a plane of symmetry)" Page 8 the draw of Histidine There is a Beta-carbon

More information

The R-subunit would not the able to release the catalytic subunit, so this mutant of protein kinase A would be incapable of being activated.

The R-subunit would not the able to release the catalytic subunit, so this mutant of protein kinase A would be incapable of being activated. 1. Explain how one molecule of cyclic AMP can result in activation of thousands of molecules of glycogen phosphorylase. Technically it takes four molecules of cyclic AMP to fully activate one molecule

More information

Exam 3 Fall 2015 Dr. Stone 8:00. V max = k cat x E t. ΔG = -RT lnk eq K m + [S]

Exam 3 Fall 2015 Dr. Stone 8:00. V max = k cat x E t. ΔG = -RT lnk eq K m + [S] Exam 3 Fall 2015 Dr. Stone 8:00 Name There are 106 possible points (6 bonus points) on this exam. There are 8 pages. v o = V max x [S] k cat = kt e - ΔG /RT V max = k cat x E t ΔG = -RT lnk eq K m + [S]

More information

3/1/2011. Enzymes. Enzymes and Activation Energy. Enzymes Enzyme Structure and Action. Chapter 4 Outline. Enzymes

3/1/2011. Enzymes. Enzymes and Activation Energy. Enzymes Enzyme Structure and Action. Chapter 4 Outline. Enzymes Free content 3/1/2011 Chapter 4 Outline Enzymes as catalysts Control of enzyme activity Bioenergetics Enzymes 4-2 4-3 Enzymes Enzymes - function as biological catalysts permit reactions to occur rapidly

More information

Exam 3 Fall 2011 Dr. Stone

Exam 3 Fall 2011 Dr. Stone Exam 3 Fall 2011 Dr. Stone Name rate forward = k forward [reactants] K eq = [products] CH 3 COOH Ka = 1.78 x10-5 -2 H 2 P0 4 = 3.98 x 10-13 rate reverse = k reverse [products] [reactants] H 3 P0 4 Ka =

More information

3) How many different amino acids are proteogenic in eukaryotic cells? A) 12 B) 20 C) 25 D) 30 E) None of the above

3) How many different amino acids are proteogenic in eukaryotic cells? A) 12 B) 20 C) 25 D) 30 E) None of the above Suggesting questions for Biochemistry 1 and 2 and clinical biochemistry 1) Henderson Hasselbalch Equation shows: A) The relationship between ph and the concentration of an acid and its conjugate base B)

More information

BASIC ENZYMOLOGY 1.1

BASIC ENZYMOLOGY 1.1 BASIC ENZYMOLOGY 1.1 1.2 BASIC ENZYMOLOGY INTRODUCTION Enzymes are synthesized by all living organisms including man. These life essential substances accelerate the numerous metabolic reactions upon which

More information

An Introduction to Enzyme Structure and Function

An Introduction to Enzyme Structure and Function An Introduction to Enzyme Structure and Function Enzymes Many reactions in living systems are similar to laboratory reactions. 1. Reactions in living systems often occur with the aid of enzymes. 2. Enzymes

More information

CH395 G Exam 2 Multiple Choice - Fall 2004

CH395 G Exam 2 Multiple Choice - Fall 2004 C395 G Exam 2 Multiple Choice - Fall 2004 1. Which of the following fatty acids has the lowest melting point? a. Fatty acids with sites of unsaturation with cis double bonds b. Fatty acids with sites of

More information

Exam II - Review Questions

Exam II - Review Questions Name Exam II - Review Questions 1. In 1962 the Nobel Prize in chemistry was shared by two researchers, each who succeeded in determining the three-dimensional structure for a protein. Who were these two

More information

Lecture 13 (10/13/17)

Lecture 13 (10/13/17) Lecture 13 (10/13/17) Reading: Ch6; 187-189, 204-205 Problems: Ch4 (text); 2, 3 NXT (after xam 2) Reading: Ch6; 190-191, 194-195, 197-198 Problems: Ch6 (text); 5, 6, 7, 24 OUTLIN NZYMS: Binding & Catalysis

More information

BCH 4053 THIRD EXAM November 5, 1999

BCH 4053 THIRD EXAM November 5, 1999 BCH 4053 THIRD EXAM November 5, 1999 I remind you that you are bound by the Academic Honor Code. This means (1) you will not give or receive information during this exam, nor will you consult with unauthorized

More information

Biochemistry. Enzymes are used all over your body! 3.1) Enzymes-I

Biochemistry. Enzymes are used all over your body! 3.1) Enzymes-I Biochemistry 3.1) Enzymes-I Introduction to enzyme structure and function, and factors involving their actions and pathways Prof. Dr. Klaus Heese Enzymes are used all over your body! 1 What is an enzyme?

More information

Amino acids. Side chain. -Carbon atom. Carboxyl group. Amino group

Amino acids. Side chain. -Carbon atom. Carboxyl group. Amino group PROTEINS Amino acids Side chain -Carbon atom Amino group Carboxyl group Amino acids Primary structure Amino acid monomers Peptide bond Peptide bond Amino group Carboxyl group Peptide bond N-terminal (

More information

Lecture 12 Enzymes: Inhibition

Lecture 12 Enzymes: Inhibition Lecture 12 Enzymes: Inhibition Reading: Berg, Tymoczko & Stryer, 6th ed., Chapter 8, pp. 225-236 Problems: pp. 238-239, chapter 8, #1, 2, 4a,b, 5a,b, 7, 10 Jmol structure: cyclooxygenase/non-steroidal

More information

Table of contents. Author's preface. Part 1: Structure and function of enzymes

Table of contents. Author's preface. Part 1: Structure and function of enzymes Author's preface xvii Part 1: Structure and function of enzymes 1 An introduction to enzymes 1.1 What are enzymes 3 1.2 A brief history of enzymes 3 1.3 The naming and classification of enzymes 4 1.3.1

More information

Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions

Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions A cell does three main kinds of work: Chemical Transport Mechanical To do work, cells manage energy resources

More information

BIOCHEMISTRY AS A SUBJECT, ITS TASKS. ENZYMES: STRUCTURE, COMMON PROPERTIES, MECHANISM OF ACTION AND CLASSIFICATION

BIOCHEMISTRY AS A SUBJECT, ITS TASKS. ENZYMES: STRUCTURE, COMMON PROPERTIES, MECHANISM OF ACTION AND CLASSIFICATION THE MINISTRY OF PUBLIC HEALTH OF UKRAINE ZAPORIZHZHIA STATE MEDICAL UNIVERSITY BIOCHEMISTRY DEPARTMENT BIOCHEMISTRY AS A SUBJECT, ITS TASKS. ENZYMES: STRUCTURE, COMMON PROPERTIES, MECHANISM OF ACTION AND

More information

l Citric acid cycle 1_ Pyruvate formation

l Citric acid cycle 1_ Pyruvate formation Chemistry 255 (Fal115) Name S 1-...e.pha.., CCrrt Exam 2 (So pts) 1. (5 pts) List the order of the metabolic events from start (#1) to fmish (#5): A TP produced in Glycolysis l Citric acid cycle 1_ Pyruvate

More information

Syllabus for BASIC METABOLIC PRINCIPLES

Syllabus for BASIC METABOLIC PRINCIPLES Syllabus for BASIC METABOLIC PRINCIPLES The video lecture covers basic principles you will need to know for the lectures covering enzymes and metabolism in Principles of Metabolism and elsewhere in the

More information

Terminology-Amino Acids

Terminology-Amino Acids Enzymes 1 2 Terminology-Amino Acids Primary Structure: is a polypeptide (large number of aminoacid residues bonded together in a chain) chain of amino acids linked with peptide bonds. Secondary Structure-

More information

Final Exam Chemistry 391 Structural Biochemistry Fall Do not open the exam until ready to begin! Rules of the Game:

Final Exam Chemistry 391 Structural Biochemistry Fall Do not open the exam until ready to begin! Rules of the Game: Name Practice for 2018 Final Exam Chemistry 391 Structural Biochemistry Fall 2016 Do not open the exam until ready to begin! ules of the Game: This is a take-home Exam. The exam is due on Thursday, December

More information

SC/BIOL Biochemistry

SC/BIOL Biochemistry SC/BIOL 2020.03 Biochemistry Midterm #1 Name: Student ID: Feb 7 th, 2013 Time: 1 hr and 15 min This test has multiple choice: 24 Marks. Fill in the blanks: 10 Marks Peptide structure: 6 Marks There are

More information

Lecture 34. Carbohydrate Metabolism 2. Glycogen. Key Concepts. Biochemistry and regulation of glycogen degradation

Lecture 34. Carbohydrate Metabolism 2. Glycogen. Key Concepts. Biochemistry and regulation of glycogen degradation Lecture 34 Carbohydrate Metabolism 2 Glycogen Key Concepts Overview of Glycogen Metabolism Biochemistry and regulation of glycogen degradation Biochemistry and regulation of glycogen synthesis What mechanisms

More information

Quiz 4 Review Guide Fall 2018

Quiz 4 Review Guide Fall 2018 Quiz 4 Review Guide Fall 2018 Major Topics: Enzyme Kinetics: o reaction rates and catalysis; transition state binding theory o Michaelis-Menten equation and interpretation o Inhibitors types and explanations

More information

Lecture 19: Review of regulation

Lecture 19: Review of regulation Chem*3560 Lecture 19: Review of regulation What is meant by cooperative allosteric regulation? Positive cooperativity - characteristic is the sigmoidal binding/activity curve T-state has weaker affinity,

More information

Answer three from questions 5, 6, 7, 8, and 9.

Answer three from questions 5, 6, 7, 8, and 9. BCH 4053 May 1, 2003 FINAL EXAM NAME There are 9 pages and 9 questions on the exam. nly five are to be answered, each worth 20 points. Answer two from questions 1, 2, 3, and 4 Answer three from questions

More information

VELOCITY OF ENZYME-CATALYZED REACTIONS.

VELOCITY OF ENZYME-CATALYZED REACTIONS. Lecture 12: Enzymes: Inhibition [PDF] Reading: Berg, Tymoczko & Stryer, Chapter 8, pp. 225-236 Problems: pp. 238-239, chapter 8, #1, 2, 4a,b, 5a,b, 7, 10 Updated on: 2/21/07 at 9:00 pm (deleted problems

More information

SYLLABUS MBMB/CHEM/BCHM 451b 2013 This class meets from pm every Tuesday and Thursday in Room 1059 (Auditorium) LS III.

SYLLABUS MBMB/CHEM/BCHM 451b 2013 This class meets from pm every Tuesday and Thursday in Room 1059 (Auditorium) LS III. 1 SYLLABUS MBMB/CHEM/BCHM 451b 2013 This class meets from 12.35-1.50 pm every Tuesday and Thursday in Room 1059 (Auditorium) LS III. FACULTY P. M. D. Hardwicke, Room 210W, Neckers "C" Wing, Tel. 618-453-6469;

More information

The effects of ph on Type VII-NA Bovine Intestinal Mucosal Alkaline Phosphatase Activity

The effects of ph on Type VII-NA Bovine Intestinal Mucosal Alkaline Phosphatase Activity The effects of ph on Type VII-NA Bovine Intestinal Mucosal Alkaline Phosphatase Activity ANDREW FLYNN, DYLAN JONES, ERIC MAN, STEPHEN SHIPMAN, AND SHERMAN TUNG Department of Microbiology and Immunology,

More information

Student number. University of Guelph Department of Chemistry and Biochemistry Structure and Function In Biochemistry

Student number. University of Guelph Department of Chemistry and Biochemistry Structure and Function In Biochemistry University of Guelph Department of Chemistry and Biochemistry 19356 Structure and Function In Biochemistry Midterm Test, March 3, 1998. Time allowed, 90 min. Answer questions 120 on the computer scoring

More information

ENZYME INHIBITION. CHM333 LECTURES 16 & 17: 10/9 16/09 FALL 2009 Professor Christine Hrycyna

ENZYME INHIBITION. CHM333 LECTURES 16 & 17: 10/9 16/09 FALL 2009 Professor Christine Hrycyna ENZYME INHIBITION - INHIBITORS: Interfere with the action of an enzyme Decrease the rates of their catalysis Inhibitors are a great focus of many drug companies want to develop compounds to prevent/control

More information

Chapter 23 Enzymes 1

Chapter 23 Enzymes 1 Chapter 23 Enzymes 1 Enzymes Ribbon diagram of cytochrome c oxidase, the enzyme that directly uses oxygen during respiration. 2 Enzyme Catalysis Enzyme: A biological catalyst. With the exception of some

More information

Mohammad Alfarra. Faisal Al Nemri. Hala Al Suqi

Mohammad Alfarra. Faisal Al Nemri. Hala Al Suqi 25 Mohammad Alfarra Faisal Al Nemri Hala Al Suqi Review: - Modes of regulation:- Feed-back regulation is when an enzyme present early in a biochemical pathway is regulated by a late product of the pathway.

More information

Exam 2 Review Problems DO NOT BRING TO EXAM

Exam 2 Review Problems DO NOT BRING TO EXAM This packet contains problems from old exams, your book, supplemental materials, and even stuff from a TA from many years past. Use this as practice only. This is not, by any means, a definitive indication

More information

Biochemistry and Physiology ID #:

Biochemistry and Physiology ID #: BM 463 Your Name: Biochemistry and Physiology ID #: Final Exam, December 18, 2002 Prof. Jason Kahn You have 115 minutes for this exam. It is worth 250 points, so you are getting more points per minute

More information

MCB 102 Discussion, Spring 2012

MCB 102 Discussion, Spring 2012 MB Discussion, Spring 2012 Practice Problems 1. Effect of enzymes on reactions Which of the listed effects would be brought about by any enzyme catalyzing the following simple reaction? k 1 S P where K

More information

THE UNIVERSITY OF MANITOBA. DATE: Oct. 22, 2002 Midterm EXAMINATION. PAPER NO.: PAGE NO.: 1of 6 DEPARTMENT & COURSE NO.: 2.277/60.

THE UNIVERSITY OF MANITOBA. DATE: Oct. 22, 2002 Midterm EXAMINATION. PAPER NO.: PAGE NO.: 1of 6 DEPARTMENT & COURSE NO.: 2.277/60. PAPER NO.: PAGE NO.: 1of 6 GENERAL INSTRUCTIONS You must mark the answer sheet with pencil (not pen). Put your name and enter your student number on the answer sheet. The examination consists of multiple

More information

From Structure to Function (II): Enzyme Structure & Catalysis

From Structure to Function (II): Enzyme Structure & Catalysis BCHS 6229 Protein Structure and Function Lecture 5 (Oct 25, 2011) From Structure to Function (II): Enzyme Structure & Catalysis 1 Outline Catalysis: Overview Active site geometry Proximity and ground-state

More information

CHEM 160A Final Exam. 1. (5 points) What factors influence an enzyme s substrate specificity?

CHEM 160A Final Exam. 1. (5 points) What factors influence an enzyme s substrate specificity? CHEM 160A Final Exam December 17, 2004 Name (1 point) 1. (5 points) What factors influence an enzyme s substrate specificity? 2. (4 points) Why are cofactors required for some enzymatic reactions? 3. (5

More information

Chemistry 135, First Exam. September 23, Chem 135, Exam 1 SID:

Chemistry 135, First Exam. September 23, Chem 135, Exam 1 SID: Chemistry 135, First Exam September 23, 2015 This exam will be worth 15% of your overall grade. Please read all instructions/questions carefully and provide answers in the space provided. There should

More information

Enzymes Biological Catalysts Review

Enzymes Biological Catalysts Review Enzymes Biological Catalysts Review Catalyst a substance that speeds up a reaction but is not actually a part of the reaction nor changes because of the reaction Catalysis the process of speeding a chemical

More information

2) At physiological ph (7.0), what is the net charge of this peptide? (note this only requires knowing the R groups on each amino acid)

2) At physiological ph (7.0), what is the net charge of this peptide? (note this only requires knowing the R groups on each amino acid) page1 (of10) Proteins and peptides (9 points) Behold, a license plate! It is from a custom classic car (ca. 1940) on display at Simpson s Nursery in Jamul, which has many plants and a remarkable collection

More information

Chem Lecture 8 Carbohydrate Metabolism Part I: Glycolysis

Chem Lecture 8 Carbohydrate Metabolism Part I: Glycolysis Chem 352 - Lecture 8 Carbohydrate Metabolism Part I: Glycolysis Introduction Carbohydrate metabolism involves a collection of pathways. Glycolysis Hexoses 3-Carbon molecules Gluconeogenesis 3-Carbon molecules

More information

Section 5. Enzymes, Equilibrium, Energy and the Sulfonamides

Section 5. Enzymes, Equilibrium, Energy and the Sulfonamides Section 5 Enzymes, Equilibrium, Energy and the Sulfonamides Monday: ESKAPE handout describing them (Tiffany will provide). M-W Tie the metabolism back to the nutritional requirements and media choice,

More information

BIOLOGY 103 Spring 2001 MIDTERM LAB SECTION

BIOLOGY 103 Spring 2001 MIDTERM LAB SECTION BIOLOGY 103 Spring 2001 MIDTERM NAME KEY LAB SECTION ID# (last four digits of SS#) STUDENT PLEASE READ. Do not put yourself at a disadvantage by revealing the content of this exam to your classmates. Your

More information

BY: RASAQ NURUDEEN OLAJIDE

BY: RASAQ NURUDEEN OLAJIDE BY: RASAQ NURUDEEN OLAJIDE LECTURE CONTENT INTRODUCTION MOST ENZYMES ARE PROTEINS ENZYME CLASSIFICATION AND NUMENCLATURE HOW ENZYMES WORK: ACTIVE SITE STRUCTURE OF THE ACTIVE SITE MODELS OF SUBSTRATE BINDING

More information

Enzymes. Enzyme Structure. How do enzymes work?

Enzymes. Enzyme Structure. How do enzymes work? Page 1 of 6 Enzymes Enzymes are biological catalysts. There are about 40,000 different enzymes in human cells, each controlling a different chemical reaction. They increase the rate of reactions by a factor

More information

PROTEOMICS August 27 31, 2007 Peter D'Eustachio - MSB

PROTEOMICS August 27 31, 2007 Peter D'Eustachio - MSB PROTEOMICS August 27 31, 2007 Peter D'Eustachio - MSB 328 e-mail: deustp01@med.nyu.edu GOALS OF THIS SEGMENT OF THE COURSE Recognize the structures of the 20 amino acids; understand their properties as

More information

Glycolysis. Degradation of Glucose to yield pyruvate

Glycolysis. Degradation of Glucose to yield pyruvate Glycolysis Degradation of Glucose to yield pyruvate After this Lecture you will be able to answer: For each step of glycolysis: How does it occur? Why does it occur? Is it Regulated? How? What are the

More information

CHM333 LECTURES 16 & 17: 2/22 25/13 SPRING 2013 Professor Christine Hrycyna

CHM333 LECTURES 16 & 17: 2/22 25/13 SPRING 2013 Professor Christine Hrycyna ENZYME INHIBITION - INHIBITORS: Interfere with the action of an enzyme Decrease the rates of their catalysis Inhibitors are a great focus of many drug companies want to develop compounds to prevent/control

More information

Lecture 18 (10/27/17) Lecture 18 (10/27/17)

Lecture 18 (10/27/17) Lecture 18 (10/27/17) Reading: Ch6; 225-232 Lecture 18 (10/27/17) Problems: Ch5 (text); 2 Ch6 (study guide-facts); 5, 6, 7, 14 NEXT Reading: Ch5; 164, 166-169 Problems: none Remember Monday at 6:30 in PHO-206 is the first MB

More information

Extracellular Enzymes Lab

Extracellular Enzymes Lab Biochemistry Extracellular Enzymes Lab All organisms convert small organic compounds, such as glucose, into monomers required for the production of macromolecules; e.g., Building Blocks Monomers Macromolecules

More information

ENZYMES. A protein with catalytic properties due to its power of specific activation Paul Billiet ODWS

ENZYMES. A protein with catalytic properties due to its power of specific activation Paul Billiet ODWS ENZYMES A protein with catalytic properties due to its power of specific activation Chemical reactions Chemical reactions need an initial input of energy = THE ACTIVATION ENERGY During this part of the

More information