Biochemistry II

BIOCHEMISTRY II
(20 pages)
Faculty of Medicine, University of Rijeka
Cours: Biochemistry II
Course Coordinator: Dijana Detel, MD, PhD, Associate professor
Colaborators: Marin Tota, PhD, Associate professor
Jelena Marinić, PhD, Assistant professor
Lara Batičić, PhD, Assistant professor
Jadranka Varljen, PhD, Full professor
Iva Potočnjak, Mag. Env. Pub. Health, PhD, Assistant
Lidija Šimić, Mag. Env. Pub. Health, Assistant
Department: Department of Medical Chemistry, Biochemistry and Clinical Chemistry
Study: Integrated Undergraduate and Graduate University Study of Medicine in English
Year of the study: Second
Academic year: 2020./2021.
COURSE SYLLABUS
Course information (basic description, general information, teaching overview, required equipment
and preparation, etc.)
Biochemistry II is a compulsory course at the second year of the Integrated Undergraduate and Graduate
University Study of Medicine in English. It consists of 42 hours of lectures, 34 hours of seminars, and 34
hours of laboratory practicals, overall 110 hours (9 ECTS). Lectures and seminars are held in lecture halls
of the Faculty of Medicine according to the course schedule. Laboratory practicals are held at the
Department of Medical Chemistry, Biochemistry and Clinical Chemistry.
The goal of teaching Biochemistry is to understand how the human body works at the molecular level: how it
uses energy, how it keeps its structure, how does it recognize different signals and respond to them, how it
develops and grows, and how it protects against disease. The focus is on the integrative function of tissues
and organs. This curriculum forms biochemical basis of physiology and offers the student the knowledge
necessary for understanding biochemical basis of many pathobiochemical processes and diseases.
Understanding these principles should help students and physicians in using the appropriate biochemical
diagnostic procedure in order to improve health, in disease prevention, and in treatment of disorders at any
human age.
Thorough the seminary part, students will gradually acquire and connect topics related to course aims.
Students will acquire knowledge and experience in basic laboratory techniques and analytical clinical
methods related to physiological and pathological states of the organism thorough laboratory practicals.
Content of the course

01. Introduction
02. Enzymes
03. Bioenergetics
04. Metabolism of carbohydrates
05. Metabolism of lipids
06. Structure and function of DNA and RNA
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07. Hormon action and signal transduction
08. Biological membranes and cellular signaling
09. Metabolism of proteins and amino acids
10. Vitamins
11. Oxidative stress
12. Integration of Metabolism
13. Biomedical importance of serum enzymes and proteins
Required literature:
1. VW. Rodwell et all.: Harpers Illustrated Biochemistry, 30th edition, The McGraw –Hill Education,
New York 2015.
2. Č. Milin et. all.: Handbook for seminars and Laboratory practicals in Biochemistry II, Department of
Chemistry and Biochemistry Faculty of Medicine, University of Rijeka, 2019.
Recommended for additional reading:

1. JM. Berg et all: Biochemistry, 8th edition, W.H. Freeman and Company, New York, 2012.
2. DL. Nelson, MM. Cox: Lehninger Principles of Biochemistry, Fourth Edition
Course teaching plan:

The list of lectures (with the titles and learning outcomes):
L1 Importance of biochemistry in understanding health and disease and the application of
biochemistry in clinical practice.
Understanding the aim of the course. Recognizing the role of Biochemistry in health care.
L2-3 Enzymes. Classification of enzymes. The kinetics of enzyme catalysis. Regulation of
enzymatic activity.
To explain the structure and the function of enzymes. To explain the structure and the function of catalytic
centers. To describe the kinetics and the mechanism of enzyme-catalyzed reactions. To define and
describe mechanisms of enzymatic activity regulation.
L4 Digestion and absorption of carbohydrates.
To list carbohydrates that appear in the food and carbohydrates that are final products of digestion
(hydrolysis catalyzed by an enzyme) being transported into enterocytes. To describe enzymes that catalyze
hydrolytic cleavage of oligosaccharides and polysaccharides.
L5-6 Metabolic pathways of carbohydrates. Glycolysis. Aerobic and anaerobic glycolysis.
Regulation of glycolysis.
To explain anaerobic and aerobic glycolysis pathways and state their final products. To show glycolysis
schematically, list glycolysis enzymes, calculate the balance of ATP formation on the substrate level by
"aerobic" glycolysis of glucose and glycogen, to describe NAD+ and NADH + H+ roles in the glycolysis,
glyceraldehyde-3-P oxidation, and pyruvate reduction. To describe the cellular location of anaerobic
glycolysis. To describe and discuss the regulation of glycolysis.
L7 Oxidative decarboxylation of keto acids.
To show sum equation of oxidative phosphorylation of pyruvate into acetyl-CoA; list all the enzymes,
coenzymes, and cofactors involved in the formation of acetyl-CoA from pyruvate and insert them in the
metabolic scheme; to state the number of ATP moles generated by formation of acetyl-CoA from one mole
pyruvate; to explain the (non)possibility of pyruvate formation from acetyl-CoA.
L8-9 Citric Acid Cycle. Regulation of Citric Acid Cycle.
To state the basic role of citric acid cycle (Tricarboxylic Acid Cycle); to show the cycle schematically, to
state cycle reactions’ cellular locations; to state reactions by which terminal oxidations occur together with
corresponding enzymes and coenzymes; to state citric acid. To list regulatory enzymes and reactions
catalysed by those enzymes.
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L10 Gluconeogenesis. Cory cycle.
To describe gluconeogenesis, to define molecules that enter the gluconeogenesis pathway, to display
glucose and glycogen formation from proteins and lipids, to list phosphatase involved in gluconeogenesis
but not in glycolysis; to state reversible glycolysis reactions, to state allosteric enzymes involved in
gluconeogenesis regulation.
L11-12 Metabolism of Glycogen. Regulation of Glycogen Metabolism.
To describe glycogen formation from glucose through glucose-l-P, and to explain the role of UTP and UDP
in that reaction; to schematically show glycogen breakdown in glucose-1-P and its hormonal regulation
(hormones, receptors, enzymes, second messengers), to explain the chemical background of glycogen
breakdown disorders.
L13 The penthose phosphate pathway.
Schematically show direct oxidation of glucose-6-P into CO2 and H2O in the pentose phosphate pathway; to
state the most important compounds of oxidative and non-oxidative phase; coenzymes that appear in the
oxidative phase dehydrogenases, to explain the role of pentose phosphate pathway – formation of NADPH+
H+ and ribose and their role in metabolism; intermediate compounds that appear both in glycolysis and
gluconeogenesis forming the link between those metabolic pathways. To explain the biochemical
mechanism and clinical correlation of glucose-6-phosphate dehydrogenase deficiency.
L14-15 Bioenergetics. Oxidative Phosphorylation.
To describe oxidative phosphorylation and electron transport chain, the location of electron transport chain
and its topology. To explain the coupling of oxidation of reduced coenzymes with the synthesis of ATP. To
explain the ATP synthase mechanism and the regulation of the oxidative phosphorylation.
L16 Digestion and absorption of lipids.
To list the part of the digestive tract where lipolytic breakdown of triacylglycerols (lipids and oils) takes place
and the factors that stimulate this breakdown; to describe the intraluminal process of triacylglycerol
breakdown concerning pancreatic lipase specificity and the action of bile salts; to describe the triacylglycerol
metabolism inside enterocytes.
L17-19 Mobilisation of fatty acids. Oxidation of fatty acids. Biosynthesis of fatty acids.
To explain how triacylglycerols (lipids) from adipose tissue serve as organism energy reservoir. To describe
the processes by which fatty acids are transported through the blood. To explain processes of fatty acid
activation and transport into the matrix of the mitochondria. To describe the catabolism of fatty acids and
their cellular location.
To calculate energy balance of fatty acid breakdown. List the essential fatty acids and their characteristics.
To describe the reaction catalyzed by acetyl-CoA carboxylase and understand the mechanisms by which its
activity is regulated to control the rate of fatty acid synthesis. To explain reactions of fatty acid biosynthesis
and the role of the multienzyme complex in that process.
L20-21 Biosynthesis of triacylglycerols and phospholipids. Glycolipids.
To outline the general structure of triacylglycerols, phospholipids, and glycerosphingolipids and indicate
their functions. To explain glycerol origin for the glycerolipid biosynthesis. To explain the role of
phospholipases in the degradation and remodeling of phospholipids. To display the phosphatidylcholine,
phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol and cardiolipin metabolism; to display
sphingomyelin and glycosphingolipid metabolism; to explain the chemical background of sphingolipid
metabolism disorders; to describe and to explain the eicosanoid structure, biological role, and metabolism.
L22-23 Biosynthesis and metabolism of cholesterol. Biosynthesis and metabolism of bile acids.
To explain the importance of cholesterol as an essential structural component of cell membranes, as a
precursor of steroid hormones, bile acids, and vitamin D. To identify stages of cholesterol biosynthesis from
acetyl-CoA. Understand the role of 3-hydroxy-3-methylglutaryl CoA reductase in controlling the rate of
cholesterol synthesis and explain the mechanisms by which its activity is regulated. To display cholic,
glycocholic, and taurocholic acid biogenesis (bile acids); to state physical and chemical characteristics and
biosynthesis of C17, C19, and C21 steroid hormones.
L24 Classification and role of lipoproteins in the metabolism.
To count transport pathways of lipids and their metabolites from enterocytes to other parts of organism; to
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define lipoproteins, to count basic types of lipoproteins and state their chemical content, to state their role in
exogenous and endogenous lipid transport; to explain the chemical background of lipoprotein metabolism
disorders. Indicate major types of apolipoprotein found in different lipoprotein classes.
L25 Metabolism of xenobiotics.
To define xenobiotics and to explain the biomedical significance of xenobiotic metabolism. To explain the
role of liver cells in the detoxification of xenobiotics. To state and explain the reactions of phase I and II. To
explain the role of cytochrome P450 and reactions catalyzed by various enzymes.
L26-27 Nucleic acid structure and function. RNA synthesis, processing, and modification.
Regulation of gene expression.
To describe the structure and function of nucleic acids; to explain semiconservative replication of DNA,
transcription, and protein biosynthesis (translation). Understand the flow of genetic information from DNA to
RNA to proteins.
L28-29 Protein synthesis. Transport of proteins. Ubiquitination of proteins.
To explain the aim and effects of posttranslational modifications of protein on structure, biochemical activity,
and intracellular traffic and sorting of proteins (trans-membrane proteins, peripheral membrane proteins,
glycosylphosphatidylinositol anchored proteins); to state the examples; to explain membrane lipids and
proteins mobility. To describe the role of ubiquitin in protein degradation.
L30 Midterm exam
L31 Protein metabolism. Digestion and absorption of proteins.
To understand the proteolysis in the digestive tract and the absorption of amino acids in the intestine; to
know extracellular proteases and their classification (exopeptidase, endopeptidase, aminopeptidase,
carboxypeptidases, dipeptidylpeptidases), to know the location of action of proteolytic enzymes, the
activation and mechanisms of pepsin, trypsin, and chymotrypsin action.
L32-33 Metabolism of amino acids. Decarboxylation, transamination and oxidative deamination.
To name and know the basic pathways of amino acid degradation (decarboxylation, transamination,
oxidative deamination); to explain the reaction of amino acid decarboxylation, name enzymes and co-
enzymes; to list biologically important amines. To explain the processes of oxidative deamination of amino
acids, formation of keto acids and ammonia, specify oxidoreductases that catalyze reactions and
coenzymes; to explain the formation of ammonia in the combined processes of transamination and oxidative
deamination resulting in glutamate; to explain the mechanism of transaminase action.
L34 Urea cycle
To indicate from which compounds high-energy carbamoyl phosphate is formed, schematically show
intermediates of urea cycle and urea formation; to identify the subcellular locations of the enzymes that
catalyses the cycle; to explain the utilization of ATP.
L35-37 Signal molecules. Role in the regulation of metabolism. Receptors and signal transduction.
Hormonal regulation of metabolism.
To explain the principles of cellular signaling. To list the signal molecules according to solubility. To explain
the role of receptors in signal transduction. To describe the classification of hormones. To explain the
mechanisms of hormone action and the hierarchy of hormones. To explain the role of receptors and G
proteins as well as the generation of second messengers in hormone signal transduction. To explain the
hormonal regulation of cellular processes through activation of cAMP and phospholipase C. To understand
the mechanism of steroid hormone action; to explain the mechanism of eicosanoids action. To list MAP
kinases pathway; to explain the role of the transcription factor NF-κB.
L38-39 Regulation of metabolic pathways.
Integrate the metabolic destiny of a food ingredient from its digestion and absorption to complete
degradation or conversion into an intermediate product. To describe the peculiarities of metabolic processes
present in skeletal muscle, fatty tissue, liver, and brain.
L40-41 Biomedical importance of plasma enzymes.
To understand the biological and diagnostic importance of serum proteins and enzymes; alanine and
aspartate aminotransferase (ALT and AST), glutamate dehydrogenase (GLDH), -glutamiltransferase
(GT), cholinesterase (CHE), creatine kinase (CK), alkaline phosphatase (ALP), lactate dehydrogenase
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(LDH), lipase, and amylase. To know the application and the role of enzymes in the diagnosis and clinical
practice.
The list of seminars (S) with descriptions:

S1 Enzymes
To explain the kinetics and the mechanism of enzyme-catalysed reactions. To describe and to explain the
regulation of enzymatic activity.
S2 Cofactors. Water soluble vitamins.
To classify and to describe the structure of cofactors. To explain the modalities of coenzyme action. To
explain the role of water-soluble vitamins in enzymatic activity.
S3 Biochemically important reactions.
To indicate, explain the physiological role and mechanism of biochemically important reactions.
S4 Carbohydrate metabolism. Regulation of gluconeogenesis.
To describe the conversion of galactose, mannose, and fructose into glucose (monosaccharide
interconversion); to state enzymes (and coenzymes) involved in the enzyme catalyzed epimerization of
galactose into glucose; to explain the chemical background of galactose metabolism disorders; to show and
to explain fructose metabolism, to explain the chemical background of fructose metabolism disorders.
S5 Function and structure of respiratory chain complexes.
To illustrate the structure of the respiratory chain. List respiratory chain complexes involved in the transfer of
electrons. To explain the mechanism of electron transfer and chemiosmotic hypothesis. Understand the role
of ubiquinone cycle and synthesis of ATP.
To classify enzymes and cofactors according to the type of catalysed reaction. To explain the role of specific
cofactor in biocatalysis.
S6 Free radicals, oxidative stress, and antioxidants’ structure and nature.
To explain the mechanisms of formation and the role of free radicals as well as the mechanisms of free
radicals’ elimination.
S7 Fat soluble vitamins.
To explain the biological role of vitamins in human health. To explain the structure, principal functions, and
metabolism of fat-soluble vitamins A, D, E, K. To explain the role of vitamin A in the metabolism of
rhodopsin (rhodopsin biosynthesis), gene expression, and tissue differentiation. To describe the metabolism
of vitamin D in the skin, liver, and kidney. To explain the role of vitamin D in the control of calcium
homeostasis. To explain vitamin E antioxidative properties in cell membranes and plasma proteins. To
describe the role of vitamin K in blood clotting
S8 Metabolism of lipids.
To name and understand the structure and chemistry of physiologically important lipids. To define the
meaning of the term lipids, and to explain their distribution according to their role and structure; to know the
most important representatives of elementary and complex lipids, biological important steroids, biological
important terpenes. To identify essential fatty acids and to explain their characteristics. To explain the
biosynthesis of polyunsaturated fatty acids. To identify ketone bodies, to describe the reaction by which they
are formed and used as a fuel for extrahepatic tissues. Identify pathological conditions when ketosis and
ketoacidosis occur. To explain biochemical mechanism and biochemical aspects of clinical disorders of
lipoprotein metabolism.
S9 Metabolism of iron, porphyrins and bile pigments.
To describe the mechanism of iron absorption, distribution, and storage into tissues. To describe the
physiological and clinical role of transferrin, ferritin, iron concentration in serum, and hepcidin in the human
organism. To explain the causes and clinical picture of iron deficiency. To explain the pathway of porphyrin
biosynthesis. To describe the causes and clinical picture of various porphyrias.
S10 Metabolic functions of the liver.
To know and explain synthetic, metabolic, and excretory function of the liver. To explain the mechanisms of
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heme degradation. To explain metabolic degradation pathway of bilirubin, name and explain related
metabolic disorders. To know the synthesis of bile acids.
S11 Catabolism of carbon skeletons of amino acids. Metabolic transformation of individual
amino acids.
To describe metabolic pathways for glycine, serine, aspartic and glutamic acid, arginine, histidine,
phenylalanine, tyrosine, tryptophan, cysteine catabolism; metabolic scheme of aromatic amino acid
degradation. To explain the mechanism of phenylketonuria, alcaptonuria, albinism, and disease of
metabolism of branched-chain amino acids.
S12 Plasma proteins and their physiological, biochemical, and diagnostic functions. Biomedical
importance of plasma proteins.
To indicate the composition and the role of blood. To classify plasma proteins. To list and explain the
separation methods of plasma proteins. To indicate the causes of changes in the concentration of plasma
proteins. To specify and distinguish acute phase proteins. To know the application and the role of
haptoglobin, ceruloplasmin, α2-macroglobulin, transferrin, α1-fetoprotein, α1-antitrypsin, fibrinogen, and α1-
acid glycoprotein in the disease diagnosis and clinical practice. To clarify the diagnostic value of serum
proteins in the case of α1–antitrypsin deficiency.
The list of laboratory practicals (LP) with short explanations:

LP1 Methods in biochemistry
To explain the principle of the methods used in biochemical laboratories (chromatography, mass
spectrometry, immunochemical methods (ELISA), western blot, DNA analysis). Apply High Performance
Liquid Chromatography (HPLC) to separate the analyte in the mixture.
LP2 Factors affecting enzymatic activity
To explain the influence of pH and temperature on the ALP enzymatic activity. To explain how substrate
concentration and inhibitor affect the rate of enzyme-catalyzed reaction.
LP3 Qualitative and quantitative analysis of carbohydrates
To apply a qualitative reaction to detect carbohydrates in biological samples. To measure serum glucose
concentration, interpret, and explain the results.
LP4 Electrophoresis of lipoproteins
To apply spectrophotometry and electrophoresis in order to determine serum lipid profile. Apply qualitative
methods for the detection of pathological components of urine.
LP5 Determination of iron concentration in serum
To determine parameters of iron status. To apply qualitative methods for the detection of pathological
components of urine.
LP6 Determination of non-protein nitrogen compounds
To measure urine and serum renal function parameters, interpret the results, and explain possible causes of
hyperuricemia and urinary infections. Apply qualitative methods for the detection of pathological
components in the urine.
LP7 Determination of clinically important enzymes
To determine serum activities of ALT, AST, ALP, CHA, and -GT and to relate their activity with specific
physiological and pathological processes.
LP8 Clinical laboratory
LP9 Midterm exam
Student obligations:
Class attendance, including test attendance, is mandatory. Students may be absent from 30% of each form
of teaching provided they have a justifiable cause. If a student is absent for more than 30% of the classes,
he/she will have to re-enroll the course.
Absence from seminars is compensated by an oral colloquium. Students are expected to actively participate
in all aspects of the course, complete laboratory reports on time, and attend the examinations. Moreover,
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preparation of the course content, which is going to be discussed during seminars and laboratory practicals,
is obligatory. During laboratory practicals, a student is obligated to wear a lab coat, to have tools (a wiping
pad, a ruler, and a calculator), and the Handbook for seminars and practicals in Biochemistry II.
Exam (exam taking, detailed exam description of the oral/written/practical part, point distribution,
grading criteria):
Student grading will be conducted according to the current Ordinance on Studies of the University of Rijeka
(approved by the Senate) and the Ordinance on Student Grading at the Faculty of Medicine in Rijeka
(approved by the Faculty Council).
Assessment of the student work
Student work will be assessed and graded during the course and on the final exam. During the course,
students may obtain a total of 100 grade points (credits). Students can achieve up to 70% of the final grade
during the classes, and a maximum of 30% of the final grade at the final exam.
Evaluation of students’ progress during classes, midterms, and the final exam in academic year 2020/2021
is shown in Table 1.
Table 1. Distribution of grade points in the course “Biochemistry II“
Evaulation Grade points
Midterm exam I 18
Midterm exams Midterm exam II 18
Midterm exam III 18
Total 54
Laboratory
Completed practical and accepted written report 8
practicals
Seminars Active participation/short written exams 8
TOTAL 70
Written exam (30 questions) 15
Final exam Oral exam 15
Total 30
TOTAL 100
Written midterm exams
During the semester, three written midterm exams are planned, which will include the content of lectures,
seminars, and laboratory practicals.
At each midterm exam, the maximum of grade points that a student can obtain is 18.
All written midterm exams consist of 40 multiple choice questions and are evaluated according to the criteria
shown in Table 2. In order to obtain grade points, a student should have/gain a minimum 50% of correct
answers on each midterm exam. Settled midterm exams are valid for the current academic year in which
they are placed.
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Table 2. Evaluation of written midterm exams I-III
Grade
% of correct answered questions
points/credits
50.00 – 54.99 9
55.00 – 59.99 10
60.00 – 64.99 11
65.00 – 69.99 12
70.00 – 74.99 13
75.00 – 79.99 14
80.00 – 84.99 15
85.00 – 89.99 16
90.00 – 94.99 17
95.00 – 100.00 18
Correction of the midterm exams
A student can access the correction of the midterm exams if he/she i) did not obtain a minimum criteria
(50% on each midterm) or ii) is not satisfied with the obtained credits and iii) in case of absence at the
midterm exam due to a justified reason.
If a student retakes the midterm exam because he/she is not satisfied with the obtained grade points, only
the credits gained from the retaken midterms will be considered.
Evaluation of the midterm corrections will be performed according to the criteria shown in the Table 2.
Students will have the opportunity to correct one or more midterm exam only once. Correction of the
midterm exam I-III will be held after completing regular class in terms set by the course schedule.
Laboratory practicals
A student can gain 8 credits throughout laboratory practicals. Evaulation of laboratory practicals implais
precisely completed experimental part of laboratory practical (maximum of 4 grade points) and completed
and accepted written report (maximum of 4 grade points).
During laboratory practicals, the oral examination of the student can be performed by the teacher.
Seminars
Throughout the course, 12 seminars are planned during which students can achieve 8 grade points.
A student can obtain a maximum of 6 grade points through short written exams and additional 2 grade
points through active participation.
Final exam
The final exam is mandatory and comprises written and oral assessment. During the final exam, students
can gain a maximum of 30 credits, 15 credits in the written part and 15 credits during the oral assessment.
Students are required to meet the minimum criteria for both parts of the final exam.
The written and the oral part of the final exam cover the entire course content.
The written part of the final exam consists of 30 multiple choice questions. In order to meet minimum criteria
and earn grade points, students must have 50% of correctly solved questions.
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Achievements during the written part of the final exam will be converted into grade points according to the
criteria shown in Table 3. In case when a student did not achieve the minimum criteria on the written part of
the final exam, attending the final exam on the following exam term is mandatory.
Assessment of the oral part of the final exam:

7.5 credits: minimum criteria satisfied
8 - 9 credits: average criteria satisfied with noticeable errors
10 – 12 credits: answer with a few errors
13 – 15 credits: outstanding answer.
In order to pass the final exam, a student must achieve at least 50% of positive answers on both written and
oral parts of the final exam.
If the student is not satisfied with the final grade, he/she may refuse the grade. In case a student does not
accept the grade, he/she must re-enter the final exam.
Table 3. Evaulation of the written part of a final exam
Grade
% of correct answered questions
points/credits
50.00 – 59.99 7.5
60.00 – 64.99 8
65.00 – 69.99 9
70.00 – 74.99 10
75.00 – 79.99 11
80.00 – 84.99 12
85.00 – 89.99 13
90.00 – 94.99 14
95.00 – 100.00 15
Conditions for admission to the final exam
A student who accomplishes 35 or more grade points during all course classes can access the final exam.
If a student achieves less than 35 grade points during all course classes, correction of the midterm exams
will be organized.
A student who achieves less than 35 grade points during all course classes even after the correction of the
midterm exams, or is absent for more than 30% of all forms of classes, is graded as unsuccessful (F) and
must re-enter the course.
Final grade
The final grade represents a sum of all grade points obtained during all course classes and on the final
exam. Students are evaluated according to the ECTS (A-F) and numerical (1-5) system.
The ECTS and the numerical grading system are defined by the following criteria:
A (5) 90 - 100 credits
B (4) 75 - 89.99 credits
C (3) 60 - 74.99 credits
D (2) 50 - 59.99 credits
F (1) 0 - 49.99 credits
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Other important information regarding the course:
Teaching is held at the prescribed time and it is not possible to enter after the teacher enters. Food and
beverages are not permitted in the classroom or in the laboratory. This includes plate lunches, drinks,
candies, etc., whether opened or not. Likewise, cell phones are not allowed in the classroom during the
midterm or final exams. Students must arrive on time for exam attendance. Anyone late for more than 15
minutes may be refused to undertake the exam.
Academic Honesty
It is expected that all students and teachers follow the code of academic honesty in accordance with the
Code of ethics for the students of the Faculty of Medicine at the University of Rijeka.
Please read the policy regarding academic honesty at:
http://medical-studies-in-english.com/wp-content/uploads/2016/12/CODE-OF-ETHICS.pdf
Contact information
For questions and concerns, please feel free to contact us by e-mail or via the Department website.
If you want to speak with a teacher during office hours (each working day between 11:00 am and 13:00 am),
please let us know by e-mail or in class.
Dijana Detel, MD, PhD, Assistant professor

e-mail: [email protected]
Marin Tota, PhD, Associate professor

Jelena Marinić, PhD, Assistant professor

Lara Batičić, PhD, Assistant professor

Iva Potočnjak, PhD, Mag. Env. Pub. Health, Assistant

Lidija Šimić, Mag. Env. Pub. Health, Assistant

Expected competencies at course enrollment:

Students are expected to have basic knowledge of biology and chemistry.
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COURSE SCHEDULE for academic year 2020./2021.
Laboratory Practicals
Date Lectures (L) Seminars (S) Lecturer
(LP)
1st week L1
02/10/2020 11:00-12:00 D. Detel, Associate professor
Lecture room 1
LP1 (group I
06/10/2020 I.Potočnjak, PhD, Assistant
and II)08:00-
11:00*
LP1 (group III and L. Batičić, Assistant professor
06/10/2020 IV)12:00- L. Šimić, Assistant
15:00*
LP1 (group V) I.Potočnjak, PhD, Assistant
06/10/2020
16:00-19:00
L2,3
Lecture room 1*
2th week S1 (group I)
Lecture room 6*
S1 (group II)
Lecture room 9*
L4
14/10/2020 12:00-13:00 J. Marinić, Assistant professor
Lecture room 1*
L5,6
Lecture room 1*
3rd week S2 (group I)
19/10/2020 08:00-10:30 I.Potočnjak, PhD, Assistant
Lecture room 6*
LP2 (group I
20/10/2020 I.Potočnjak, Assistant
and II)08:00-
11:00*
20/10/2020 L. Šimić, Assistant
IV)12:00-
15:00*
20/10/2020
16:00-19:00
L7
21/10/2020 12:00-13:00 J.Varljen, Full professor
Lecture room 1*
S2 (group II)
22/10/2020 13:00-15:30 I.Potočnjak, Assistant
Lecture room 9*
L8,9
23/10/2020 10:00-12:00 J.Varljen, Full professor
Lecture room 15*
Lecture room 6*
11
S3 (group II)
Lecture room 6*
L10
Lecture room 8*
L11,12
Lecture room 1*
12
Lecture room 6*
LP3 (group I
and II)08:00-
11:00
LP3 (group III and L.Batičić, Assistant professor
3/11/2020
IV)11:00-14:00 L. Šimić, Assistant
3/11/2020
16:00-19:00
L13
Lecture room 1*
S4 (group II)
Lecture room 6*
L14,15
6/11/2020 10:00-12:00 M.Tota, Associate professor
Lecture room 8*
09/11/2020 08:00-10:30 L. Batičić, Assistant professor
Lecture room 6*
S5 (group II)
Lecture room 5*
L16,17
Lecture room 8*
Midterm exam I
13/11/2020 10:00 – 11:00
Lecture room 2
Lecture room 7*
S6 (group II)
Lecture room 4*
L18,19
Lecture room 1*
Lecture room 4*
L20,21
Lecture room 1*
S7 (group II)
Lecture room 5*
L22,23
Lecture room 1*
Lecture room 9*
13
LP4 (group I
and II)08:00-
11:00
14
IV)12:00-15:00
1/12/2020
16:00-19:00
L24
Lecture room 1*
S8 (group II)
Lecture room 7*
L25,26
J. Marinić, Assistant professor
4/12/2020 10:00-12:00
Lecture room 1* L. Batičić, Assistant professor
07/12/2020 08:30-11:00 D. Detel, Associatet professor
Lecture room 9*
L27
09/12/2020
12:00-13:00 L. Batičić, Assistant professor
Lecture room 8*
S9 (group II)
10/12/2020
11:00-13:30 D. Detel, Associate professor
Lecture room 6*
L28,29
Lecture room 15*
11th week LP5 (group I and II)
I.Potočnjak, PhD, Assistant
15/12/2020 08:00-10:30
15/12/2020 LP5 (group IiI and L. Batičić, Assistant professor L.
IV)11:00-13:30 Šimić, Assistant
15/12/2020 LP5 (group V) I.Potočnjak, PhD, Assistant
16:00-19:00
L30
Lecture room 1*
L31 Midterm exam II
Lecture room 2
Lecture room 9*
S10 (group II)
Lecture room 4*
L 32,33
Lecture room 8*
7/1/2021 12:30-15:00 J.Marinić, Assistant professor
Lecture room 9*
L34,35
D. Detel, Associate professor
8/1/2021 10:00-12:00
Lecture room 1* J.Marinić, Assistant professor
Lecture room 7*
15
S11 (group II)
Lecture room 7*
16
LP6 (group I
and II)08:00-
11:00
LP6 (group III i
IV)12:00-
15:00
LP6 (group V)
16:00-19:00
L36,37
Lecture room 1*
S12 (group II)
Lecture room 9*
L38,39
15/1/2021 10:00-12:00 D.Detel, Associate professor
Lecture room 1*
15th week LP7 (group I
19/1/2021 and II)
08:00-11:00
LP7 (group III and L.Batičić, Assistant professor
19/1/2021
IV) L. Šimić, Assistant
12:00-15:00
LP7 (group V) L. Šimić, Assistant
19/1/2021
16:00-19:00
L40,41
20/1/2021 11:00-13:00 D.Detel, Associate professor
Lecture room 1*
S13 (group I and II) D.Detel, Associate professor
21/1/2021 J.Marinić, Assistant professor
14:00-16:00
16th week LP8 (group I and II)
LP8 (group III L.Batičić, Assistant professor
26/1/2021
and IV)
8:00-11:00
LP8 (group V) L. Šimić, Assistant
27/1/2021
08:00-11:00
Midterm exam III
27/1/2021 (the time and place of the exam will be announced)
CORRECTION TEST I-III
9/2/2021
(the time and place of the exam will be announced)
CORRECTION TEST I-III
23/2/2021 (the time and place of the exam will be announced)
*Taking into consideration the current epidemiological situation of COVID-19, during the winter semester of
the academic year 2020/2021 the lectures and seminars will be held online at given time (e.g. through the
MS Teams app).
According to the course coordinator decision, specific lectures and seminars will be held on site. Possible
changes in the course timetable will be announced in advance. Students are expected to regularly check the
Merlin platform for updates.
17
List of lectures, seminars, and laboratory practicals:
Teaching
Topics of the Lectures Lecture Room
Hours
Importance of biochemistry in understanding health and disease
L1 1 1
and the application of biochemistry in clinical practice.
Enzymes. Clasification of enzymes. The kinetics of enzyme
L2 1 1
catalysis.
L3 Regulation of enzymatic activity. 1 1
L4 Digestion and absorption of carbohydrates 1 1
L5 Metabolic pathways of carbohydrates. Glycolysis. 1 1
L6 Regulation of glycolysis. 1 1
L7 Oxidative decarboxylation of ketoacids. Oxidation of pyruvate. 1 1
L8 The Citric acid cycle: degradation of acetyl-CoA. 1 15
L9 Regulation of the citric acid cycle. 1 15
L10 Gluconeogenesis. 1 8
L11 Metabolism of Glycogen. 1 1
L12 Regulation of glycogen metabolism. 1 1
L13 The penthose phosphate pathway. 1 1
L14 The respiratory chain. 1 8
L15 Energetics and principles of the respiratory chain. 1 8
L16 Digestion and absorption of lipids. 1 8
L17 Fat mobilization. 1 8
L18 Oxidation of fatty acids. 1 1
L19 Biosynthesis of fatty acids. 1 1
L20 Biosynthesis of triacyglycerols and phospholipids. 1 1
L21 Glycolipids: structure, biosynthesis, and biodegradation. 1 1
L22 Biosynthesis and metabolism of cholesterol. 1 1
L23 Biosynthesis and metabolism of bile acids. 1 1
L24 Lipoproteins. Classification and its role in metabolism. 1 1
L25 Metabolism of xenobiotics. 1 1
L26 Nucleic acid structure and function. 1 1
L27 Replication. RNA synthesis. Regulation of gene expression. 1 8
L28 Protein syntesis. Posttranslational modification of proteins. 1 15
L29 Intracellular traffic and sorting of proteins. 1 15
L30 Metabolism of proteins. Digestion and absorption of proteins. 2 1
L31 Midterm exam 1 2
L32 Metabolism of amino acids. Decarboxylation. 1 8
L33 Transamination. Oxidative deamination. 1 8
L34 Urea cycle. 1 1
L35 Signal molecules. 1 1
L36 Receptors and signal transduction. 1 1
18
L37 Hormonal regulation of metabolism. 1 1
L38 Regulation of metabolic pathways. 1 1
L39 Relationships in intermediary metabolism. 1 1
L40 Clinical importance of AST, ALT, GLDH, GT, and CHE. 1 1
L41 Clinical importance of CK, ALP, LDH, lipase, and amylase. 1 1
Total number of lectures 42
Teaching Lecture Room

Topics of Seminars (S)
Hours
2nd week Group I: 6
Enzymes 2
S1 Group II: 9
3trd week Group I: 6
Cofactors. Water soluble vitamins. 3
S2 Group II: 9
4th week Group I: 6
Biochemically important reactions 2
S3 Group II: 6
5th week Group I: 6
Metabolism of carbohydrates 2
S4 Group II: 6
6th week Function and structure of respiratory chain Group I: 6
3
S5 complexes Group II: 5
7th week Free radicals, oxidative stress, and antioxidants’ Group I: 7
3
S6 structure and nature Group II: 4
8th week Group I: 4
Fat soluble vitamins. 2
S7 Group II: 5
9th week Group I: 9
Metabolism of lipids 3
S8 Group II: 7
10th week Group I: 9
S9 Metabolizam of iron, porphyrins, and bile pigments 3
Group II: 6
12th week Group I: 9
Function of the liver in metabolism 3
S10 Group II: 4
13th week Catabolism of carbon skeletons of amino acids. Group I: 9
3
S11 Metabolic transformation of individual amino acids. Group II:7
14th week Plasma proteins and their physiological, Group I: 7
S12 3
biochemical, and diagnostic functions Group II: 9
15th week
Oral colloqium and Consultation(s) 2
S13
Total 34
19
Teaching Lecture Room
Topics of Laboratory Practicals (LP) Hours
1st week
Methods in biochemistry 4 Online
LP1
3rd week Factors affecting enzymatic activity
LP2 The influence of pH, temperature, and substrate
4 Online
concentration on the enzymatic activity. Determination of
the type of enzyme inhibition.
5th week Qualitative and quantitative analysis of carbohydrates Department of
LP3 Quantitative determination of glucose in blood. 4 Chemistry and
Detection of glucose in urine. Biochemistry
9th week Electrophoresis of lipoproteins
LP4 Quantitative determination of triglycerides in serum. Department of
Detection of ketone bodies in urine. 4 Chemistry and
Determination of total cholesterol in serum. Biochemistry
Determination of serum HDL and LDL cholesterol in serum.
11th week Determination of iron concentration in serum Department of
LP5 Determination of TIBC and UIBC. 3 Chemistry and
Detection of hemoglobin/bilirubin in urine. Biochemistry.
14th week Determination of non-protein nitrogen compounds: Department of
LP6 urea, creatinine, and uric acid in urine. 3 Chemistry and
Detection of nitrites in urine. Biochemistry
15th week Department of
Determination of clinically important enzymes:
LP7 4 Chemistry and
ALT, AST, ALP, CHE, and Gt.
Biochemistry
16th week Clinical laboratory Clinical Hospital Center
LP8 Biological material and processing in clinical bichemistry 4 Rijeka
Biochemical results and and their interpretation
LP9 Midterm exam 4
Total 34
Final exam dates

1. 11.02.2021.
2. 25.02.2021.
3. 08.07.2021.
4. 02.09.2021.
5. 16.09.2021.
20

Biochemistry II

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BIOCHEMISTRY II

Content of the course

Recommended for additional reading:

Course teaching plan:

The list of seminars (S) with descriptions:

The list of laboratory practicals (LP) with short explanations:

Assessment of the student work

Table 1. Distribution of grade points in the course “Biochemistry II“

Evaulation Grade points

Written midterm exams

Correction of the midterm exams

Assessment of the oral part of the final exam:

Table 3. Evaulation of the written part of a final exam

Conditions for admission to the final exam

Dijana Detel, MD, PhD, Assistant professor

Marin Tota, PhD, Associate professor

Jelena Marinić, PhD, Assistant professor

Lara Batičić, PhD, Assistant professor

Iva Potočnjak, PhD, Mag. Env. Pub. Health, Assistant

Lidija Šimić, Mag. Env. Pub. Health, Assistant

Expected competencies at course enrollment:

Teaching Lecture Room

Final exam dates

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