AAU
KING ABDULAZIZ UNIVERSITY
ACADEMIC ASSESSMENT UNIT
COURSE PORTFOLIO
FACULTY OF SCIENCE
DEPARTMENT BIOCHEMISTRY
COURSE NAME: General Metabolism
COURSE NUMBER:BIOC (312)
SEMESTER/YEAR: First semester / 1429-1430H
DATE: 11/2/2009 16/2/1430H
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PART I
INSTRUCTORS & GENERAL
INFORMATION
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PART II
COURSE SYLLABUS
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Instructor Information
1. Dr. Wadiah Saleh Backer
Office location: [Bldg. 7, Room 2- 114]
Phone: 640-1000 Ext.63191
Email: wbacker@kau.edu.sa
Office hours: Sunday: 1 – 2.30, Tuesday: 10 – 2.30, Wednesday : 11- 1
2. Dr. Karima Sayed Ahmed Osman Mohamed
Office location: [Bldg. 7, Room 012-2]
Phone: 640-1000 Ext.63633
Email: karimasao@hotmail.com
Office hours: Saturday and Monday: 9 – 11, Sunday &Tuesday: 9-11.30
Welcome to this course
General Metabolism [Bioc 312]
The course is designed to familiarize the student with the basic principles of protein metabolism and
related compounds. I expect each student to apply diligently themselves to learn this course which
will enable them to understand a lot of diseases and basic science that related to biochemistry.
I promise to serve you as facilitator and mentor, but you must do the learning. Study outside of class
time, faithfully work the assignments, and try to understand the information presented. Don’t hesitate
to ask and contact me at office hours if you face any difficulty. I will be happy to help you over the
hard parts but you must do the work.
I hope every student enjoy studying this course with my best wishes for all of you to get a good
mark.
Good luck.
Course Information
General Metabolism II (Bioc.) 312 SA & SB (2+1 cr. Hr. Lab.):
SA
Dr. Wadiah Saleh Backer
Building :7
Room : B-74
Time : 9 : 9:50 S.T.
SB
Dr. Karima Sayed Ahmed Osman Mohamed
Building :7
Room : B-115
Time :8 : 8:50 S.M.
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Course prerequisites and requirements General Biochemistry (Bioc. 211)
Course Description
Different pathways of biosynthesis and catabolism of protein and nucleotides. The course include four
chapter as follow:
1. Metabolism of proteins and amino acids
2. Catabolism of the carbon skeletons of amino acids
3. Conversion of amino acids to specialized products
4. Metabolism of nucleotides
Course Objectives
1. Students will learn and understand the major metabolism of protein, amino acids and nucleotides
and their biochemical importance in the metabolic map.
2. To study the general amino acids pool and general utilization of amino acids.
3. To describe different metabolic pathway of individual amino acid.
4. To identify the different enzymes reactions involved in urea and uric acid formation.
5. To describe the mechanisms used to control the pathway.
6. To describe the metabolic effects of different diseases.
7. To describe the role of some biochemical compounds that amino acids form and related disease.
8. To describe the clinical significance of some biochemical compounds that amino acids form.
Specific objective for each chapter are contained in the lecture handout.
Learning Resources
Main Text Book
Biochemistry (2005), 3rd edition, Pamela C. Champe and Richard A. Harvey, J. B. Lippincott Company,
Philadelphia.
General Text-Books
1. Biochemistry (2004), 3rd edition, Donald Voet and Judith Voet , John Whiley and Sons, Inc., New
York.
2. Understanding nutriton (2005), 10th edition., Whitney, E. & Rolfes, S. R., Thomson & Wadsworth.
3. Lenninger Principles of Biochemistry (2000), David L. Nelson and Michel M. Cox.,Worth
Pubishers, New York
4. Harper's Biochemistry (2003), 26th edition, Robert K. Murray, Daryl K. Granner, Petter A. Mayes
and Victor W. Rodwell, McGraw-Hill, Newyork.
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5. Wills' Biochemical Basis of Medicine (2000), 3rd edition, Brain Gillhan, Despo K and J. Hywel
Thomas, Butterworth-Heinemann, Oxford.
6. Biochemistry illustrated (2000), 4th edition, Peter N. Campbell and Anthony D. Smith, Churchill
Livingstone, Edinburgh London.
7. Medical Biochemistry (1999), John Baynes and Mark H. Doiniczak. Mosby, London.
8. Biochemistry (1996). Robert Roskoski, W. B. Saunders Company, Philadelphia.
.
9. Biochemistry (1995), 4th edition, Stryer L. W. H. Freeman, New York.
10. Biochemistry (1993),3rd edition, Zuby.Wm. C. Brown, Oxford, England.
Other text are potentially acceptable, Please speak and discussed with me if you currently own different
Biochemistry text book.
Type of Quizzes and Exams
Examination will consist of various types of questions:
Examination will consist of:
a) Multiple choices.
b) True/false.
b) Short answers.
c) Fill in the blanks
d) Match colunms.
The questions will be derived from lecture material and chapters in the textbook.
The goal of exams to challenge the student to draw from information presented through out the
lectures and text book.
Ideal answer will be discussed in class with the students after correction.
Notes:
ُ1- Exam date according to the timetable.
2- Missed exams will be given only in extraordinary circumstances. It cannot be made up without
acceptable report from the collage and without prior arrangement.
3- Cheating is not acceptable. Any episodes of cheating will be dealt with according to collage
and university policy.
4- Class attendance is important. The students are required for all materials for missed class
periods.
The students are expected to fully participate in class. Absence are disruptive and will impair
your progress. Please be on time for class.
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Course Grading
For final grades, you are guaranteed the following grades [A+, A, B+, B, C+, C, D+, D and F] if your
final percentage lies indicated range:
95-100 % A+
90-94%
A
85-89%
B+
80-84%
B
75-79%
C+
70-74% C
65-69%
D+
60-64%
D
< 60%
F
Usually, high grades are seen in the students who are participate in the class discussions, chare, pay
attention, active, cleaver, intelligent, and hard working. Please, study hard, prepare for class. Persist
when learning is difficult. Read and thought about materials. Translate all that into academic
success.
Methods of evaluation % of grade:
Exam1
15%
Quiz
5%
Exam 2
15%
Laboratory
25%
Final exam
40%
------------------------------------------------------------------------------Total
100
Course Schedule Model
(meeting two times a week)
Week #
Lecture
1
Introduction to the Course,
Proteins and Amino Acids
Date the Exam̉s Time
2
- Structure of 20 Amino Acids
- Classes of Amino Acids
- Essential and Nonessential
- Protein Turnover
-The Biological Value of Dietary
Proteins
1
Digestive Tract Nitrogen
(Digestion of Dietary protein).
1
2
Topic
Reading
Assignment
What is Due?
Buy Book 
Chapter 1
Memorize the
Structure of 20
Amino Acids
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Week #
Lecture
2
1
3
- The Glutamine Synthetase
Reaction
- D-Amino acid oxidase
1
- Urea Cycle
- Regulation of Urea Cycle
2
- The overall Reaction of Urea
Cycle
- Qiuz
1
Urea Cycle Defects (UCDs)
Fate of Urea
Sources of Ammonia
2
Exam 1
5
1
Reading
Assignment
Absorption and Transport of
Amino Acids
1. Active Transport for L-Amino
Acids
A) Carrier Protein Transport
System
B) Glutathione Transport System
2. Passive transport
3 Ttransported of Amino Acids
into Cell.
Removal of Nitrogen from
Amino Acids
1) Transaminations
2) Oxidative Deamination
2
4
6
Topic
What is Due?
Review the
previous lecture
Review the
previous lecture
Review the
previous lecture
Review the
previous lecture
- Answer Exam 1
- Ammonia Toxicity
(Hyperammonemia).
- Ammonia in the Circulation
- Overall Nitrogen Metabolism
Chapter 2
Metabolism of carbon skeletons of amino acids
6
2
Metabolic Fate of Amino Acid
Carbon Skeletons
A. Reamination by ammonia
B. Catabolized to form seven products
-Glucogenic and ketogenic Amino
Acids
Review the
previous lecture
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Week #
Lecture
1
7
2
Topic
Reading
Assignment
A. Amino Acids Forming Pyruvate
1. Glycine Forming Pyruvate
2. Alanine Forming Pyruvate
(Glucose-alanine cycle)
3. Serine Forming Pyruvate
4. Cysteine Forming Pyruvate
5. Threonine Forming Pyruvate
6. Tryptophan Forming Pyruvate
B. Amino Acids Forming α- Ketoglutarate
1. Glutamine Forming α- Ketoglutarate
2. Glutamate Forming α- Ketoglutarate
3. Arginine Forming α- Ketoglutarate
4. Proline Forming α- Ketoglutarate
5. Histidine Forming α- Ketoglutarate
What is Due?
Review the
previous lecture
Review the
previous lecture
1
C. Amino Acids Forming Oxaloacetate
(Asparagine and Aspartate)
D. Amino Acids Forming Fumarate
and Acetoacetyl CoA
(Phenylalanine and Tyrosine)
1. Phenylketonuria.
2. Tyrosinemia.
3. Alkaptonuria.
4. Albinism.
Review the
previous lecture
2
E. Amino Acids Forming Succinyl
CoA
1.Methionine Forming Succinyl CoA.
I. Homocystinuria
II- Cystathioninuria
Review the
previous lecture
8
1
9
2
2. Valine and Isoleucine Forming
Succinyl-CoA
3. Threonine Forming Succinyl-CoA
G. Amino Acids Forming Acetyl
CoA and Acetoacetyl CoA
Amino Acid Biosynthesis
1. Biosynthesis of Glutamate/
Glutamine and Aspartate/Asparagine.
2. Biosynthesis of Alanine
3.Biosynthesis of Cysteine
4.Biosynthesis of Tyrosine
5. Biosynthesis of Proline
6. Biosynthesis of Serine
7. Biosynthesis of Glycine
Review the
previous lecture
Review the
previous lecture
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Week #
Lecture
Topic
Reading
Assignment
What is Due?
Chapter 3
Conversion of Amino Acids to Specialized Products
10
1
2
Introduction
1. Synthesis of Porphyrins Heme
1. Structure of Heme
2. Synthesis of Heme
3. Degradation of Heme
Jaundice
Types of jaundice
1
11
12
13
a) Hemolytic jaundice
b) Obstructive jaundice
c) Hepetocellular jaundice
d) Jaundice in Newborns
Determination of bilirubin
concentration
Review the
previous lecture
2
Creatine
1. Synthesis of Creatine
2. Function of Creatine
3. Degradation of Creatine
Histamine
Synthesis and Function of Histamine
Melanin
Review the
previous lecture
1
Compounds Tryptophan Synthesize
 Serotonin.
 Melatonin.
 Niacin (nicotinic acid)/Pellagra
 Indol and skatol.
Review the
previous lecture
2
Mid-term Exam
1
Catecholamines
 Functions of Catecholamines
 Synthesis of Catecholamine
 Degradation of Catecholamines
Glutathione
1. Glutathione Sturcture
2. Functions of Glutathione
Review the
previous lecture
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Week #
Lecture
2
Reading
Assignment
Topic
Thyroid Hormones
Formation of Tri-iodothyronine (T3)
and Tetra-iodothyronine (Thyroxine,
T4).
Cofactors that Used in Amino Acids
Metabolism
1. Folic Acid
2. Biopterin
What is Due?
Review the
previous lecture
Chapter 4
14
1
Nucleotide Metabolism
Answer Mid-term Exam
 Nucleotide structure (Purine and
Primidine)
 Degradation of Dietary Nucleic
Acids
 Conversion of Ribonucleotides to
Deoxyribonucleotides
 Biosynthesis of Purine
1. De novo purine nucleotide
synthesis
A. Synthesis of 5-Phosphoribosyl-1pyrophosphate (PRPP)
B. Synthesis of 5'-Phosphoribosylamine
C. Synthesis of Inosine
Monophosphate
2
D. Conversion of IMP to AMP and
GMP
E.Conversion of Nucleoside
Monophosphate to Di- and Triphosphate
F. Inhibitors of Purine Synthesis
G. Regulation of Biosynthesis of
Purine Nucleotides
II. Purine Salvage Pathway
Review the
previous lecture
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Week #
Lecture
Topic
Reading
Assignment
What is Due?
 Catabolism of Purine
Nucleotides
Disorders of Purine Catabolism:
a) Hyperuricemia (gout)
b) Hypouricemia
 Pyrimidine Biosynthesis
15
1
I- De novo synthesis
A. Pyrimidine Synthesis
B. Formation of a Pyrimidine
Nucleotide
C. Regulation of Pyrimidine
Nucleotide Biosynthesis
II- Pyrimidine Salvage System
Final Exam
Review the
previous lecture
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PART III
COURSE RELATED MATERIAL
Contains all the materials considered essential to teaching the
course, includes:
Quizzes, lab quizzes, mid-terms, and final exams and their solution set
Paper or data show copies of lecture notes/ handouts (optional)
Practical Session Manual (if one exists)
Handouts for project/term paper assignments
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PART IV
EXAMPLES OF STUDENT LEARNING
Examples of student work. (Included good, average, and poor
examples)
Graded work, i.e. exams, homework, quizzes
Students' lab books or other workbooks
Students' papers, essays, and other creative work
Final grade roster and grade distribution
Examples of instructor’s written feedback of student’s work, (optional)
Scores on standardized or other tests, before and after instruction,
(optional)
Course evaluation, self evaluation or students comments (optional)
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PART V
INSTRUCTOR REFLECTION (optional)
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Part V. Instructor Reflections on the Course
 Instructor feedback and reflections
 Propose future improvement and enhancement
 Evaluate student competency and reflect on their course evaluation for
improvements to the course
 Conceptual map of relationships among the content, objective, and
assessment
 Recent trends and new approaches to teach the course.
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COURSE PORTFOLIO
CHECKLIST
TITLE PAGE
COURSE SYLLABUS
COURSE RELATED MATERIAL
EXAMPLES OF EXTENT OF STUDENT
LEARNING
INSTRUCTOR REFLECTION ON THE COURSE
ACADEMIC ASSESSMENT UNIT