Preview Lippincott Illustrated Reviews Flash Cards Biochemistry by Ferrier D.R., Jameson B.A. (2015) Preview Lippincott Illustrated Reviews Flash Cards Biochemistry by Ferrier D.R., Jameson B.A. (2015) Preview Lippincott Illustrated Reviews Flash Cards Biochemistry by Ferrier D.R., Jameson B.A. (2015) Preview Lippincott Illustrated Reviews Flash Cards Biochemistry by Ferrier D.R., Jameson B.A. (2015) Preview Lippincott Illustrated Reviews Flash Cards Biochemistry by Ferrier D.R., Jameson B.A. (2015)
http://tm.firebrandtech.com/WK/WK_FileRepository/WK_IMAGES/9781451191110.jpg[5/30/2014 12:55:29 PM] Lippincott Illustrated Reviews Flash Cards BIOCHEMISTRY Denise R Ferrier, PhD Bradford A Jameson, PhD Professor of Biochemistry Department of Biochemistry and Molecular Biology Drexel University College of Medicine Philadelphia, Pennsylvania Professor of Biochemistry Department of Biochemistry and Molecular Biology Drexel University College of Medicine Philadelphia, Pennsylvania Ferrier_FM.indd i 5/3/14 4:48 AM Acquisitions Editor: Tari Broderick Product Development Editor: Stephanie Roulias Production Project Manager: David Orzechowski Design Coordinator: Holly McLaughlin Illustration Coordinator: Doug Smock Manufacturing Coordinator: Margie Orzech Prepress Vendor: Absolute Service, Inc Copyright © 2015 Wolters Kluwer Health All rights reserved This book is protected by copyright No part of this book may be reproduced or transmitted in any form or by any means, including as photocopies or scanned-in or other electronic copies, or utilized by any information storage and retrieval system without written permission from the copyright owner, except for brief quotations embodied in critical articles and reviews Materials appearing in this book prepared by individuals as part of their official duties as U.S government employees are not covered by the above-mentioned copyright To request permission, please contact Wolters Kluwer Health at Two Commerce Square, 2001 Market Street, Philadelphia, PA 19103, via email at permissions@lww.com, or via our website at lww.com (products and services) 987654321 Printed in China 978-1-4511-9111-0 1-4511-9111-1 Library of Congress Cataloging-in-Publication Data is available upon request Care has been taken to confirm the accuracy of the information presented and to describe generally accepted practices However, the author(s), editors, and publisher are not responsible for errors or omissions or for any consequences from application of the information in this book and make no warranty, expressed or implied, with respect to the currency, completeness, or accuracy of the contents of the publication Application of this information in a particular situation remains the professional responsibility of the practitioner; the clinical treatments described and recommended may not be considered absolute and universal recommendations The author(s), editors, and publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accordance with the current recommendations and practice at the time of publication However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any change in indications and dosage and for added warnings and precautions This is particularly important when the recommended agent is a new or infrequently employed drug Some drugs and medical devices presented in this publication have Food and Drug Administration (FDA) clearance for limited use in restricted research settings It is the responsibility of the health care provider to ascertain the FDA status of each drug or device planned for use in his or her clinical practice Ferrier_FM.indd ii 5/23/14 1:09 AM Features: Three-Step Review SPOT FLASH Test your grasp of key concepts or equations on a lecture-by-lecture basis! COURSE REVIEW Ensure a thorough understanding of course material through in-depth questions High-yield facts for course- and Board-exam review! CLINICAL CORRELATIONS Explain how the basic science helps predict outcomes in a clinical setting! Featuring the same visionary artwork found in Lippincott Illustrated Reviews: Biochemistry With Lippincott Illustrated Reviews, Seeing is Understanding Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_FM.indd iii Copyright © 2015 Wolters Kluwer 5/3/14 4:48 AM Ferrier_FM.indd iv 5/3/14 4:48 AM Preface Lippincott Illustrated Reviews Flash Cards: Biochemistry is a portable study tool designed for self-assessment and review of medical biochemistry The flash cards were developed primarily for use by medical students studying biochemistry and preparing for United States licensing exams, but information is presented with a clarity and level of detail that makes them ideal supplements for any of the allied health sciences The deck contains three card types: Question (Q) cards, Case cards, and Summary cards Q CARDS The majority of cards are Q cards that prompt the reader with questions (on the front) to assess level of understanding, depth of knowledge, and ability to apply biochemical concepts The answers (on the back) are more inclusive than those found on typical flash cards Most Q cards contain three questions or sets of questions on a common topic: The first tests for retention of basic facts, whereas the next two test understanding and/or application of related concepts and clinical correlations Each question type is denoted by icons SPOT FLASH: Illustration-based questions test your grasp of key facts and are intended for use on a lecture-by-lecture assessment and review basis COURSE REVIEW: In-depth questions promote a thorough understanding of related concepts The answers focus on high-yield facts to help consolidate and apply material during course- and licensing-exam review CLINICAL CORRELATIONS: Clinical questions highlight the basic science foundations of medicine They help students apply biochemical concepts to clinical problems and are particularly useful when studying for licensing exams Continued, over Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_FM.indd v Copyright © 2015 Wolters Kluwer 5/3/14 4:48 AM Preface Q cards include several features to facilitate learning and retaining the material: • Illustrations: Richly detailed illustrations from the popular companion text, Lippincott Illustrated Reviews: Biochemistry, appear on both sides of the cards Many of the illustrations include narrative boxes that guide readers through complex concepts • Notes: Answers may be supplemented with information that goes beyond the need-to-know basics to provide context or to enrich and help anchor a concept • Emphasis: Key terms, disease names, and pathologic findings are bolded for rapid review and assimilation CASE CARDS AND SUMMARY CARDS Case cards use common clinical presentations to highlight biochemical concepts Summary cards (for the vitamins and the fed/fasted states) highlight key features of these information-rich areas of medical biochemistry The card deck is designed to be comprehensive, covering all significant biochemical concepts Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_FM.indd vi Copyright © 2015 Wolters Kluwer 5/3/14 4:48 AM Acknowledgments The authors wish to thank John Swaney, PhD, our colleague at Drexel University College of Medicine, for his careful reading of the manuscript and constructive comments Any errors are ours alone We thank the publishing team assembled by Wolters Kluwer Stephanie Roulias, product development editor, and Kelly Horvath, freelance development editor, along with Doug Smock, Teresa Exley, and David Orzechowski, gave invaluable assistance in the development and production of the finished product We also thank Robin R Preston, PhD, for his design of the flash card format Dedication The authors dedicate this work to the medical, biomedical graduate, and professional studies students of Drexel University You have challenged and inspired us, and have made us better teachers Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_FM.indd vii Copyright © 2015 Wolters Kluwer 5/3/14 4:48 AM Figure Credits Card 3.6 Question and Answer: Modified photo courtesy of Photodyne Incorporated, Hartland, WI Card 4.2 Answer: Kronauer and Buhler, Images in Clinical Medicine, The New England Journal of Medicine, June 15, 1995, Vol 332, No 24, p 1611 Card 4.5 Question and Answer: Modified photo from Web site Derma.de Modified Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_FM.indd viii from Jorde LB, Carey JC, Bamshad MJ, et al Medical Genetics 2nd ed St Louis, MO: Mosby; 2000 http://medgen.genetics utah.edu/index.htm Card 13.6 Answer: From the Crookston Collection, University of Toronto Card 21.2 Answer: Modified from Rich MW Porphyria cutanea tarda Postgrad Med 1999;105:208–214 Card 21.4 Question and Answer: From Custom Medical School Stock Photo, Inc Card 22 Case Card Question: Modified from WebMD Inc http://www.samed.com/sam/ forms/index.htm Card 23.6 Question and Answer: Modified from Cryer PE, Fisher JN, Shamoon H Hypoglycemia Diabetes Care 1994;17: 734–753 Copyright © 2015 Wolters Kluwer 5/3/14 4:48 AM Contents UNIT Protein Structure and Function 1.1 UNIT Bioenergetics and Carbohydrate Metabolism 6.1 UNIT Lipid Metabolism 15.1 UNIT Nitrogen Metabolism 19.1 UNIT Metabolism Integration 23.1 UNIT Genetic Information Storage and Expression 29.1 CHAPTER 34 Blood Clotting 34.1 APPENDIX Abbreviations A-1 Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_FM.indd ix Copyright © 2015 Wolters Kluwer 5/3/14 4:48 AM 5.1 Answer Enzyme Nomenclature and Properties Shown is an enzyme that belongs to the class known as oxidoreductases (that most commonly function as dehydrogenases) NAD functions as a coenzyme–cosubstrate in enzymatic reactions because it is only loosely bound to the enzyme and leaves the enzyme in a changed form [Note: FAD is an example of a coenzyme–prosthetic group It is tightly bound to the enzyme and is returned to its original form on the enzyme.] CH3 C H COO– + NAD+ CH3 C COO– + NADH + H+ Lactate OH 2eO dehydrogenase 2H+ Lactate Pyruvate Based on its designation as a phosphorylase, myophosphorylase (deficient in McArdle disease) uses Pi to cleave bonds in glycogen Therefore, a decrease in Pi will decrease enzymatic activity [Note: The enzyme cleaves the ␣(1→4) glycosidic bond in glycogen, thereby generating the phosphorylated product glucose 1-P.] Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 52 Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.2 Question Enzyme Properties Enzymes are protein that increase the of a chemical reaction As shown, they contain an , which is a small on the surface of the enzyme to which a specific binds, forming an complex leading to product formation Binding may cause a conformational change in the enzyme, a process known as ? What is the difference between a holoenzyme and an apoenzyme? Elevated blood ALP suggests a pathology ALP is found primarily in the liver as ALP-1 and in bone as ALP-2 Levels of the two forms can help differentiate between a liver and a bone pathology What term is used to describe the tissue-specific forms of an enzyme? ? Enzyme Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 53 Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.2 Answer Enzyme Properties Enzymes are protein catalysts that increase the rate (velocity) of a chemical reaction As shown, they contain an active site, which is a small pocket (or cleft) on the surface of the enzyme to which a specific substrate binds, forming an enzyme-substrate complex leading to product formation Binding may cause a conformational change in the enzyme, a process known as induced fit [Note: RNA catalysts are referred to as ribozymes.] Substrate A holoenzyme is an enzyme with its nonprotein component, and an apoenzyme is missing the nonprotein component The nonprotein component is required for enzymic activity Isozyme (isoenzyme) is the term used to describe the tissue-specific forms of an enzyme, such as ALP-1 and ALP-2 Isozymes catalyze the same reaction but differ in their amino acid composition (primary structure) Active site Enzyme Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 54 Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.3 Question How Enzymes Work What name is given to that region of the curve shown at right marked by the asterisk (*)? Which arrow (blue or red) represents the free energy of activation of the uncatalyzed reaction? How enzymes affect the ⌬G of a reaction? Free energy (G) How enzymes dramatically increase the reaction rate relative to the uncatalyzed reaction? * A Initial state (reactants) ΔG B Final state (products) Progress of reaction Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 55 Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.3 Answer How Enzymes Work The asterisk (*) marks the transition state Free energy of activation (uncatalyzed) The blue arrow represents the free energy of activation of the uncatalyzed reaction The lower the free energy of activation, the faster the reaction rate Enzymes lower the free energy of activation by (1) providing an alternate, energetically favorable reaction pathway and (2) stabilizing the transition state of this pathway Stabilization increases the concentration of the reactive intermediate that can be converted to product, thereby increasing the reaction rate [Note: The turnover number (kcat), the number of substrate molecules converted to product per second, is increased.] T* Free energy (G) Enzymes have no effect on the ⌬G of a reaction Therefore, the free energies of the reactants and the products are the same in the catalyzed and uncatalyzed reactions Transiti Transition state A Initial state (reactants) tants) Free energy of activation (catalyzed) ΔG B Final state (products) Progress of reaction Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 56 Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM Factors Affecting Reaction Velocity 5.4 Question What processes are shown at right? What effect they have on the velocity of an enzymecatalyzed reaction? What general name is given to the enzyme that catalyzes the forward reaction? What other environmental factors influence the velocity of an enzyme-catalyzed reaction? Tyrosinemia type (infantile tyrosinemia) is caused by a deficiency in fumarylacetoacetate hydrolase that catalyzes the last reaction in the degradation of Tyr It is treated with a drug that inhibits an enzyme earlier in the pathway What is the biochemical rationale for this therapy? Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 57 ATP Enzyme ADP Enzyme 2− OP03 OH 2− HPO4 H2O Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.4 Answer Factors Affecting Reaction Velocity Phosphorylation and dephosphorylation, covalent modifications to proteins, are shown Depending on the enzyme, these modifications may increase or decrease the velocity of an enzyme-catalyzed reaction [Note: The change in enzyme activity is the result of a conformational change in the enzyme caused by the covalent modification.] ATP Protein kinase ADP Kinases catalyze phosphorylation reactions using ATP as the phosphate source They are opposed by phosphatases Changes in the concentration of the enzyme, coenzyme, and substrate; temperature; and pH are additional factors that influence the velocity of an enzyme-catalyzed reaction Nitisinone is prescribed for infantile tyrosinemia because it decreases production of the substrate for the hydrolase, thereby decreasing the velocity of the reaction Additionally, by preventing substrate accumulation, this substrate reduction therapy prevents entry of the substrate into side reactions that produce harmful products Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 58 Enzyme Enzyme 2− OP03 OH 2− HPO4 Phosphoprotein H2O phosphatase Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.5 Question Michaelis–Menten Kinetics Supply the missing terms in the Michaelis–Menten equation shown What is the steady state assumption? vo = Vmax ? Km + ? True or false: When the [S] is much less than the Km, the V0 is proportional to [S], and the reaction is said to be first order If 1/V0 and 1/[S] were plotted, what shape would result? What is the X intercept on this plot? The Y intercept? If a mutation to the gene that codes for an enzyme results in a 12-fold increase in the Km of the enzyme for its physiologic substrate, what effect has the mutation had on the affinity of the enzyme for the substrate? Lippincott Illustrated Reviews Flash Cards: Biochemistry Ferrier_Unit01.indd 59 Copyright © 2015 Wolters Kluwer 5/2/14 7:08 PM 5.5 Answer Michaelis–Menten Kinetics [S] is the missing term in the Michaelis–Menten equation [S] V vo = max Km + [S] The steady state assumption is that the concentration of ES does not change with time That is, the rate of formation of ES is equal to that of the breakdown of ES to E ϩ S and E ϩ P True: When [S] is much less than the Km, the V0 is proportional to [S], and the reaction is said to be first order, as shown Increasing the Km of the enzyme for its physiologic substrate decreases the affinity of the enzyme for the substrate Reaction velocity (vo) A straight line would be seen if 1/V0 and 1/[S] were plotted The X intercept on this Lineweaver-Burk plot is ؊1/Km, and the Y intercept is 1/Vmax Vmax Vmax 0 [Substrate] [Subst Km At low concentrations of substrate ([S]