LEBANESE INTERNATIONAL UNIVERSITY – BEIRUT CAMPUS

BIOC 310: Medical Biochemistry (4 credits)

Instructor Dr. Jamilah Borjac-Natour

Office Hours MW 9:30-10:00, 12:00-12:30Beirut
TTH 10:30-11:00 Saida campus
Lecture Hours MW 10:00-10:50 Beirut
TTh 8:30-10:20
TTH 11:00-12:50
Semester Spring 09-10

Note: Office hours will not be used to cover the material missed during the unexcused absence of the student.

GRADE DISTRIBUTION
Exam I 30% March 26th
Exam II 30% May 7th
Final Exam 40%

Note: Make up exams will not be given under any circumstance. Students with valid excuses should fill in the “Student
Excuse Form”, in the department. If the excuse form is approved, the student will sit for the missed exam along with the
following exam (excluding final exams).

COURSE DESCRIPTION
The study of human biochemistry describes how the body works, and provides a basis for understanding what can, and often
does, go wrong. From a physician's point of view, biochemistry provides not only a description of how the system works,
but also a foundation for understanding how to improve its operation through appropriate nutrition, exercise, preventive
medicine, how to diagnose problems and, where possible, how to remedy them. Current therapies include recombinant
proteins, such as human insulin or erythropoietin synthesized by bacteria, and future therapies will include genetic
engineering, involving gene rather than organ transplants. To understand how the human body works, and the basis of the
therapies for its maintenance and healing, it is essential to understand not only the chemistry of the reactions, but also the
functional interactions between metabolic pathways, organs, and tissues. This, in a broad sense, is the realm of physiologic
biochemistry.
COURSE PREREQUISITE
BIOL 200, CHEM 250

COURSE OUTCOMES

By the end of this course, the students should be able to:

1. Defining the properties and kinetics of enzymes and their regulations
2. Defining the role of hemoglobin in oxygen transport and as a blood buffer
3. Study the metabolism of carbohydrates and the mechanisms of their regulation
4. Study the role of bioenergetics and oxidative metabolism in eukaryotic cells
5. Study the metabolism of lipids , and their metabolic regulation
6. Studying the structure of amino acids, their metabolism and their relationship to carbohydrate formation
7. Studying the structures and the biosynthetic pathways of nucleotides.
8. Examine the biosynthetic pathways of eicosanoids and their role in inflammation
9. Understand the biosynthetic pathways of steroid hormones and their mode of action
10. Clinical correlations.

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REQUIRED TEXTBOOK
Medical Biochemistry by Baynes and Dominiczak, Mosby, 2nd edition, 2005. Elsevier Mosby.

REFERENCE BOOKS
Principles of Biochemistry by Horton, Moran, Ochs, and Scrimgeour (2002). 3rd edition. International Edition or Prentice
Hall Upper Saddle River, NJ 07458

Donald Voet and Judth Voet, Biochemistry, third edition, John Wiley and Sons.

Lehninger Principles of Biochemistry, Fourth Edition by David L. Nelson, Michael M. Cox, Publisher: W. H. Freeman

Biochemistry (4th edition) by Lubert Stryer.

ATTENDANCE
For legitimate reasons only, a student is allowed to absent him/herself for a maximum of 6 hours per course. However, any
absence greater than 1 hour will be counted toward the 5 % evaluation. Absences beyond the specified limit will be assessed
by the Chairman of the Department and may result in an AW or other disciplinary measures. An unexcused absence from a
drop quiz will result in a zero on that drop quiz. An unexcused absence from an exam will result in a zero on that exam.

POLICIES AND PROCEDURES

 No student is allowed to enter into the classroom after 5 minutes of the commencement of the lecture.
 Pin drop silence should be maintained in the classroom. Ill-behavior is strictly prohibited. A student will be sent
out of the classroom if he/she is found doing a mischief/cross-talk when the lecture is in progress. Remember, in such
cases, that student is marked to have an “unexcused absence” from that lecture.

HOW TO DO WELL IN THIS CLASS

 Confirm your motivation for taking the class. The reasons you come to class, read the text, and study – like the reasons
you’re in graduate school – have to be your own.
 Be prepared to work hard.
 COME TO CLASS
 Read the relevant text before class. Make a note of material that seems particularly important or that you do not fully
understand. If this material does not become clear during the lecture, ask questions.
 Be an active learner. Listen, write, ask questions and answer questions.
 Develop good study habits. I suggest dedicating at least one hour per lecture to the material. The material must be
understood and integrated with previous subjects, not just memorized. Paraphrase/expand your notes within 24 hours of
class. Draw diagrams and concept maps of how you understand the material.
 Seek the help, advice, or assistance of one of the instructors.
 Study with others and use all of the amazing resources available to you on the Web and in the library.

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COURSE OUTLINE BY TOPIC

Topics Title / Chapter Assignment # Hours

1 Amino Acid and proteins and Acid Base Balance (Chapter 2+Chapter 23)

 General structure of amino acids and other amino acid derivatives

 Ionization of amino acids
 Peptide bonds linking amino acids 5
 Protein purification techniques
 Techniques for protein composition and sequence
 What are the levels of protein structure
 Conformation of peptide group
 Protein denaturation and renaturation
 Protein folding and stability

2 Oxygen transport and Fibrous proteins (Chapter 4; pp. 35-47 and chapter 27 pp. 387-390) 3

 Structure of heme prosthetic group

 Characteristics of the mammalian globin protein
 Structure of collagen as a fibrous protein
 Structure of myoglobin and hemoglobin as a globular proteins
 Normal Hb, sickle cell disease and other hemoglobinopathies
 Oxygen binding of Hb and Mb
 Collagens and non-collagenous proteins in extracellular matrix.

3 Properties of enzymes (Chapter 5; pp. 51– 59) 4

 Classes of enzymes
 The Michealis-Menten equation
 Reversible and irreversible enzyme inhibition
 Regulation of enzyme activity
 Chemical and binding mode of enzymatic catalysis ( in brief)
 Diffusion Controlled reaction
 Properties of serine proteases
Micronutrients: Vitamins and Minerals (Chapter 10; pp. 127-139)
4 2.5
 Coenzyme classification
 Coenzymes derived from water soluble vitamins
 Coenzymes derived from lipid soluble vitamins
 Trace elements

Exam I
Carbohydrates and glycoproteins (Chapter 25+ 27; pp. 359-369)
5 3
 Monosaccharides and their derivatives, Disaccharides and other glycosides, Polysaccharides
(breief review)
 Glycoconjugates

Bioenergetics (Chapter 8; pp. 93-96)

6 2
 What are metabolic pathways
 Regulation of metabolic pathways
 Thermodynamics and metabolism
 Metabolic role of ATP and other compounds with phosphoryl group transfer ability
 Reduced coenzymes as energy conserver

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7 Glycolysis (Chapter 11; pp. 340 – 366) 4

 Description of the glycolytic pathway

 Regulation of glycolysis
 Metabolism of other monosaccharides
 Importance of 2,3 bisphosphoglycerate in RBC
 The pentose phosphate pathway

8 Carbohydrate storage and Synthesis in liver and Muscle (Chapter 12 and Chapter 20 ; pp. 157- 4.5
167 and pp. 273-294)

 Glycogen degradation and synthesis

 Regulation of glycogen metabolism
 Glucogenesis, its precursors and its regulation
 Hypoglycemia
 Diabetes Mellitus and its treatment

9 The Tricarboxylic Acid Cycle (Chapter 13; pp. 175-187) 2

 Conversion of pyruvate to acetylCoA

 Oxidation of AcetylCoA
 Regulation of the TCA cycle

10 Oxidative Metabolism (Chapter 8; pp. 96-110) 2

 The chemiosmotic theory

 The different complexes of the electron transport system
 P/O ratio
 Aerobic oxidation of the cytosolic NADH
 Regulation of oxidative phosphorylation
Exam II

11 Membrane and Transport (Chapter 7 pp. 77-80, and Chapter 26 pp. 375-379) 3

 Structural and functional diversity of lipids

 Fatty acids, triglycerides, glycerophospholipids, sphingolipids, steroids, eicosanoids,
prostaglandins and waxes.
 The biological membrane: the lipid bilayer, the fluid mosaic model of the biological membrane.
 Classes of membrane proteins
 Membrane transport
 Transduction of extracellular signals: Adenylate cyclase signaling pathway, the inositol-
phospholipid signaling pathway, receptor tyrosine kinases.

12 Oxidative Metabolism of Lipids in Liver and Muscle (Chapter 14, 15, 16 and 17; pp. 189-240) 8

 Absorption and mobilization of dietary lipids

 Lipoproteins
 Storage and mobilization of fatty acids
 Fatty acid oxidation: Even and odd saturated and unsaturated fatty acids
 Ketone bodies synthesis and oxidation
 Fatty acid synthesis
 Fatty acids elongation and desaturation
 Regulation of fatty acid oxidation
 Synthesis of eicosanoids
 Synthesis of triglycerides and glycerophospholipids
 Synthesis of cholesterol

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 13 Amino acids metabolism (Chapter 18; pp 245-259) 5

 Nitrogen cycle and nitrogen fixation

 Assimilation of ammonia
 Regulation of glutamine synthetase
 Transamination reactions
 Synthesis of non-essential amino acids
 Amino acid catabolism
 The urea cycle
 Catabolism of carbon chains of amino acids
 Renal glutamine metabolism
 Synthesis of nitric oxide from arginine
14 Biosynthesis and Degradation of Nucleotides (chapter 29; pp 413-421) 5

 De novo synthesis of purine nucleotides

 De novov synthesis of pyrimidine nucleotides
 Reduction of ribonucleotides to deoxyribonucleotides
 Salvage pathway of purines and pyrimidines
 Purine catabolism
 Pyrimidine catabolism
15 Deoxyribonucleic acid Replication and RNA transcription and Protein synthesis and turnover 7
(chapters 30, 31, 32 pp 425-447)

 Nucleotides the building blocks of nucleic acids

 Structure of DNA
 Packaging of DNA in eukaryotic cells
 DNA replication
 Process of transcription
 Protein synthesis

Final Exam

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DISCLAIMER: Changes may be performed to the above syllabus without any prior notification.