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Biochemistry Course Outline for Animal Science

The document outlines the course 'Biochemistry for Animal Science' at Dilla University, detailing its structure, learning outcomes, and course contents. Key topics include the properties of water, biomolecules, enzyme functions, metabolic pathways, and the roles of nucleic acids. Assessment methods include lab work, quizzes, mid-exams, and a final exam, with references provided for further reading.

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0% found this document useful (0 votes)
16 views4 pages

Biochemistry Course Outline for Animal Science

The document outlines the course 'Biochemistry for Animal Science' at Dilla University, detailing its structure, learning outcomes, and course contents. Key topics include the properties of water, biomolecules, enzyme functions, metabolic pathways, and the roles of nucleic acids. Assessment methods include lab work, quizzes, mid-exams, and a final exam, with references provided for further reading.

Uploaded by

majiokyienc
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd

DILLA UNIVERSITY

COLLEGE OF AGRICULTURE
Department of Animal science Course outline
Course Title: Biochemistry for animal science
Course Code: AnSc 2181
Course Credit Hours: 3 (2+1)

Course information:- Understanding and characterizing the structure, properties and metabolism
of common chemical compounds found in living organisms

Course Description:- Unique properties of Water as applied to Life, Structure and chemistry of
biomolecules (proteins, carbohydrates, lipids, nucleic acids, Minerals and Hormones); enzymology;
intermediary metabolism and generation and storage of metabolic energy; oxidative-reductive
processes; selected metabolic pathways of carbohydrates and fats; integration of metabolism, and
their roles in metabolic regulations.

Learning outcomes: -

•Explain the formulae of specified chemical compounds commonly found in organisms.

• Differentiate between characteristics of major groups of biochemicals.

• Identify differences between monosaccharides, a fat, an oil; and amino acids.

• Explain the characteristics of a specified protein formula.

• Compare fibrous proteins with globular proteins.

• Explain the functions of carbohydrates.

• Distinguish between an enzyme and a hormone

• Explain how one specific enzyme functions.

• Explain how one specific hormone functions.

• Explain the importance of RNA and DNA.

• Describe the biological and chemical differences between RNA and DNA.

• Explain the role of ATP in providing energy for various cellular activities.

• List the main biochemical processes involved in carbohydrate metabolism.

• Explain glycolysis, including the sequence of chemical reactions involved.

• Explain the Krebs cycle, including the sequence of chemical reactions involved.

Course Contents:
Chapter - 1
1. Introduction
1.1. Definition and Scope of Biochemistry
1.2. Biomolecules and the Cell
1.2.1. The Cell
1.2.2. Biomolecules
1.3. Chemical Bonds in Biochemistry

Chapter - 2
2. Water, pH, and Buffer
2.1. Introduction
2.2. Unusual properties of water to be used as a biological solvent
2.3. Role of water in biological system
2.4. Intermolecular forces
2.5. Colligative properties
2.6. Hydronium ion and pH
2.7. Physiological Buffers and buffering agent
2.8. Buffers used by cells
2.9. Some common Buffers used in biochemical reactions

Chapter-3
3. Protein Structure and Function
3.1. Structure and function of amino acids
3.2. Introduction to amino acids (essential and non-essential amino acids)
3.3. Structure of amino acids
3.4. Amino Acids as Buffers
3.5. Peptide Bond Formation (Peptide linkage)
3.6. Structure and function of Proteins
3.7. Primary Structure of Proteins
3.8. Secondary Structure of Proteins
3.9. Tertiary Structure of Proteins
3.10. Quaternary Structure of Proteins
3.11. Denaturation of Proteins
3.12. Uses of proteins

Chapter-4
4. Enzymes
4.1. Definition of Enzymes
4.2. Properties of Enzymes
4.3. Major Classes of Enzymes
4.4. Enzyme Kinetics
4.5. Enzyme Mechanism (mechanism of catalysis)
4.6. Regulation of Enzyme activity (Activation/Inhibition)

Chapter-5
5. Lipids
5.1. Definition of lipids
5.2. Different classes of lipids
5.3. Biological membranes
5.4. Membrane transports

Chapter-6
6. Carbohydrates
6.1. Definition and Classification,
6.2. Monosaccharides
6.3. Disaccharides
6.4. Polysaccharides

Chapter - 7
7. Introduction to Metabolism
7.1. Metabolic Pathways
7.2. Bioenergetics
7.3. Regulations

Chapter-8
8. Carbohydrate Metabolism
8.1. Structure of Carbohydrate
8.2. Digestion of Carbohydrate
8.3. Glycogen Metabolism
8.4. Degradation of Glycogen
8.5. Metabolism of Monosaccharides and Disaccharides
8.6. Glycolysis
8.7. Fates of Pyruvate
8.8. Energy yield of Glycolysis
8.9. Citric Acid Cycle
8.10. Electron Transport Chain and Oxidative Phosphorylation
8.11. Hexose Monophosphate Pathway (Pentose Phosphate pathway)
8.12. NADPH/Pentose
8.13. Gluconeogenesis
8.14. Reactions Unique to Gluconeogenesis
8.15. Substrates for Gluconeogenesis
8.16. Regulations of Gluconeogenesis

Chapter-9
9. Lipid Metabolism
9.1. Introduction
9.2. Metabolism of Dietary Lipids
9.3. Fatty Acid and Triacylglycerol Metabolism
9.4. Mobilization of Stored Fats and Oxidation of Fatty Acids
9.5. Phospholipid Metabolism

Chapter-10
10. Amino Acids/Nitrogen Metabolism
10.1. Nitrogen Fixation and Synthesis of Amino Acids
10.2. Digestion of Dietary Proteins
10.3. Removal of Nitrogen from Amino Acids
10.4. Urea Cycle: The Major Pathway of Disposal of Nitrogen
10.5. Amino Acids: Metabolism of Carbon Atoms
10.6. Catabolism of the Carbon Skeletons of Amino Acids
10.7. Biosynthesis of Nonessential Amino Acids
10.8. Conversion of Amino Acids to Specialized Products: An overview
Chapter-11
11. Integration of Metabolism
11.1. Metabolic Effects of Insulin and Glucagon
11.2. Starvation and fasting; similarity and differences
11.3. Nutrition
11.4. Vitamins

Chapter-12
12. Nucleic Acid Structure and Function
12.1. Structure of DNA and RNA
12.2. DNA Synthesis (Overview) (Replication)
12.3. RNA Synthesis
12.4. Protein Synthesis

Assessment:
 Lab work and report 20%
 Quizzes/assignment 15%
 Mid exam 25%
 Final exam 40%

References
1. Berg, J.M., J.L. Tymoczko and L. Stryer, Biochemistry, 5th Ed., 2005: and Student’s Companion
to Stryer’s Book.
2. Champe, P.C.; R.A. Harvey, 2007. Biochemistry, 4th Ed., Lippincott,s Illustrated Reviews.
3. Cohn E.E and P.K Stumpf. Outlines of Biochemistry John Will & Sons, Inc.
4. Elliott, WH &Elliott, DC 2001. Biochemistry and Molecular Biology, 2 nd edn, Oxford University
Press, Oxford.
5. Mathews, CK, Van Holde, KE & Ahern, K.G. 2000. Biochemistry, 3rd edn, Benjamin/Cummings
Publishing Company, 2000 (Pearson Educ)
6. Nelson, D.L., Lehninger, A.L. and Cox, M.M., 2018. Lehninger principles of biochemistry.
Macmillan.
7. Voet, D, Voet, J G & Pratt, C. W. 1998. Fundamentals of Biochemistry, John Wiley &Sons, New
York.

Common questions

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The Krebs cycle involves acetyl-CoA combining with oxaloacetate to form citrate, which undergoes a series of enzyme-catalyzed reactions producing ATP, NADH, and FADH2 while regenerating oxaloacetate . It is critical as it provides key metabolites and coenzymes for aerobic respiration, facilitating the transfer of energy-supplying electrons to the electron transport chain .

Oxidative phosphorylation occurs in the mitochondria, where electrons are transferred through the electron transport chain, creating a proton gradient across the inner mitochondrial membrane . ATP synthase then uses this gradient to synthesize ATP from ADP and inorganic phosphate, making it the cell's primary energy currency. Key components include NADH, FADH2, electron carriers, and ATP synthase .

Water acts as a solvent, facilitating the proper orientation and interaction of enzyme and substrate molecules through its polarity and hydrogen bonding capability . It participates as a reactant or product in many enzymatic reactions, stabilizing reaction intermediates and maintaining optimal conditions for enzyme activity . Its involvement is crucial for reaction flexibility and efficiency, influencing reaction rates and enzyme specificity .

Glycolysis is a ten-step process where glucose is broken down into pyruvate, yielding ATP and NADH, which are crucial for energy production in cells . It serves as the primary pathway for sugar catabolism, providing intermediates for other metabolic pathways and playing a pivotal role in both aerobic and anaerobic respiration .

Water's unique properties, such as its polarity and ability to form hydrogen bonds, make it an excellent solvent that can dissolve diverse biological molecules, facilitating biochemical reactions necessary for life . Its capacity to maintain temperature stability and act as a medium for metabolic reactions is crucial for sustaining cellular processes .

Enzyme activity regulation is crucial as it ensures metabolic pathways are responsive to cellular needs, maintaining homeostasis. For example, allosteric regulation allows enzymes like phosphofructokinase to adjust glycolysis rates in response to ATP levels . Inhibition or activation of enzymes alters pathway efficiency, optimizing resource use and energy production .

Enzymes are catalytic proteins that facilitate biochemical reactions without being consumed, characterized by specific active sites for substrate binding . Hormones are signaling molecules, often proteins or lipids, that regulate physiological processes by binding to receptors, initiating specific responses in target cells . Essential for metabolic and regulatory functions, enzymes and hormones differ in mechanisms—catalytic versus signaling .

Glucose, a monosaccharide, is a small, soluble sugar used immediately for energy via glycolysis . Glycogen, a polysaccharide, serves as a large, branched storage molecule for glucose, releasing it when needed during glycogenolysis for sustained energy supply . Glucose provides quick energy, while glycogen enables energy storage and release during varying metabolic demands .

The primary structure of proteins is the linear sequence of amino acids, dictating the protein's overall shape and function . The secondary structure, formed by hydrogen bonds, results in alpha-helices and beta-sheets, contributing to the protein's stability and folding, which are essential for its biological role . Primary structures determine the sequence of secondary structures, influencing how proteins form and function in biological systems .

Fibrous proteins have elongated structures and provide support and strength (e.g., collagen), while globular proteins possess compact, spherical shapes, enabling them to perform dynamic functions like enzyme catalysis (e.g., enzymes). The structural differences affect their solubility and functional roles, with fibrous proteins being less soluble and more stable than globular proteins, which are more versatile in cellular functions .

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