Marks' Basic Medical Biochemistry: A Clinical Approach
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5TH EDITION
About this book
It has been 5 years since the fourth edition was completed. The fifth edition has some significant organizational changes, as suggested by extensive surveys of faculty and students who used the fourth edition in their classes and studies. The major pedagogic features of the text remain. They have been enhanced by the following changes for the fifth edition:
1 . Every patient history has been reviewed and revised to reflect current standards of care (as of 2016). The patient names have also been changed to a first name and last initial. A key indicating the "old" names and "new" names is available in the online supplement associated with the text.
2. The Biochemical Comments associated with each chapter have been updated, where appropriate, to allow students to experience where current research efforts are headed.
3. The presentation of metabolism has been altered such that glycolysis is now the first topic discussed, followed by the tricarboxylic acid cycle, and then oxidative phosphorylation. The correlation between fourth edition chapters and fifth edition chapters are as follows:
a. Chapters 1 through 18, no change b. Section IV is now entitled "Carbohydrate Metabolism, Fuel Oxida tion, and the Generation of Adenosine Triphosphate" and consists of Chapters 1 9 through 28.
i. Chapter 19 of the fifth edition (Basic Concepts in the Regulation of Fuel Metabolism by Insulin, Glucagon, and Other Hormones) is based on Chapter 26 of the fourth edition.
ii. Chapter 20 of the fifth edition (Cellular Bioenergetics: Adenosine Triphosphate and 02) is based on Chapter 19 of the fourth edition.
iii. Chapter 21 of the fifth edition (Digestion, Absorption, and Trans port of Carbohydrates) is based on Chapter 27 of the fourth edition.
iv. Chapter 22 of the fifth edition (Generation of Adenosine Triphos phate from Glucose, Fructose, and Galactose: Glycolysis) is based on Chapter 22 of the fourth edition and also contains parts of Chapter 29 of the fourth edition (Pathways of Sugar Metabolism: Pentose Phosphate Pathway, Fructose, and Galactose Metabolism).
v. Chapter 23 of the fifth edition (Tricarboxylic Acid Cycle) is based on Chapter 20 of the fourth edition.
vi. Chapter 24 of the fifth edition (Oxidative Phosphorylation and Mi tochondrial Function) is based on Chapter 21 of the fourth edition.
vii. Chapter 25 of the fifth edition (Oxygen Toxicity and Free-Radical Injury) is based on Chapter 24 of the fourth edition.
viii. Chapter 26 of the fifth edition (Formation and Degradation of Glycogen) is based on Chapter 28 of the fourth edition.
ix. Chapter 27 of the fifth edition (Pentose Phosphate Pathway and the Synthesis of Glycosides, Lactose, Glycoproteins, and Glyco lipids) is based on Chapter 30 of the fourth edition, along with a section (The Pentose Phosphate Pathway) of Chapter 29 of the fourth edition. This led to the deletion of old Chapter 29 from the Table of Contents of the fifth edition.
Questions & Answers from this book
Questions and answers are connected to the referenced book and its available source material.
Chapter 8: Enzymes as Catalysts
How does substrate concentration affect the velocity of an enzyme-catalyzed reaction according to the Michaelis-Menten model?
According to the Michaelis-Menten model, as substrate concentration increases, the velocity of an enzyme-catalyzed reaction also increases until it reaches a maximum velocity (Vmax). The reaction velocity is most sensitive to changes in substrate concentration when the concentration is below the enzyme's Km, where small increases in substrate can significantly enhance the reaction rate. Once substrate concentration exceeds Km, further increases have a diminishing effect on velocity.
How does the concentration of enzyme affect the rate of a reaction according to the chapter on enzymes as catalysts?
The concentration of an enzyme affects the rate of a reaction by determining the maximum velocity (V max) of the reaction. As enzyme concentration increases, the rate of reaction can increase until it reaches V max, where all enzyme molecules are saturated with substrate. This relationship is described by the Michaelis-Menten equation, which shows that the reaction rate is most sensitive to changes in substrate concentration when it is below the enzyme's Km.
Chapter 17: Use of Recombinant DNA Techniques in Medicine
Chapter 20: Cellular Bioenergetics: Adenosine Triphosphate and O2
Chapter 22: Generation of Adenosine Triphosphate from Glucose, Fructose, and Galactose: Glycolysis
Chapter 23: Tricarboxylic Acid Cycle
Chapter 24: Oxidative Phosphorylation and Mitochondrial Function
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