Download Semmelweis University Department of Medical Biochemistry

Semmelweis University
Department of Medical Biochemistry
MEDICAL BIOCHEMISTRY & MOLECULAR BIOLOGY I.
2009-2010 Fall Semester
Department of Medical Biochemistry
Tűzoltó utca 37-47. Budapest IX., H-1094, Hungary, Europe
www.biokemia.sote.hu phone: +36-1-4591500#60010, fax: +36-1-2670031
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 1
Medical Biochemistry and Molecular Biology I
Course: Medical Biochemistry and Molecular Biology I.
Type: Compulsory
Course director: Prof. Ádám, Veronika
Code for dentist students: FOOBIBKM_1A
Code for medical students: AOOBIBKM_1A
Teaching staff:
Machovich, Raymund Prof. MD, PhD, D Sci
Mandl, József Prof. MD., D Sci, Head of the Dept. Medical Chemistry
Sasvári, Mária Prof. MD., PhD, D Sci
Tóth, Miklós Prof. MD., D Sci
Bartha, Katalin PhD.,
Chinopoulos, Christos MD., PhD.
Csala, Miklós MD, PhD
Hrabák, András PhD
Kolev, Kraszimir MD, PhD, D Sci
Komáry, Zsófia MD.
Léránt, István PhD. Tutor for the medical and dentist students
Maróthy-Tóth, Erzsébet PhD
Szabados, György MD., PhD.
Törőcsik, Beáta, MD., PhD.
Tretter, László MD., PhD, D Sci
Vér, Ágota MD., PhD
Wohner, Nikolett MD,
Teaching Secretary:
Léránt, István
Tel.: +36 (20) 6632267, +36 (20) 6660034 +36 (1) 4591500#60034
[email protected] [email protected]
Student Affairs Secretary:
Mrs Nemes, Katalin
Tel: +36 (20) 5629800 +36 (20) 6660061 +36 (1) 4591500#60061
[email protected]
Lab coordinator:
Dr. Kolev, Kraszimir
Lab Staff:
Mrs Vallinger, Éva Senior Lab. Technician
Mr Ozsváth, Zsolt Lab. Technician
Ms Mártonffy, Ildikó Lab. Technician
Course timing
Year: 2nd
Period: 1st semester
Total weeks: lecture 14 , seminar - , practical 14
Hours per week: lecture 4 , seminar - , practical 3
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 2
The aim of the course:
Biochemistry gives a comprehensive description and understanding of chemical
processes important in human body. The course treats medical aspects with
outstanding importance. The main
topic of this semester's course is the intermediary metabolism. Special emphasis is put
on the regulatory and medical aspects. Certain pathologically important chapters are
covered on seminars by the method of problem based learning in order to help students
to develop skills in applying their basic knowledge to solve real medical cases.
Content:
Intermediary metabolism
Carbohydrate metabolism
Digestion and absorbtion of carbohydrates. Pathological aspects. Lactase deficiency. The
metabolism of fructose, fructose intolerance. Galactose metabolism, galactosemias. Glucose
metabolism, overview. The pentose phosphate pathway. Pathological aspects.
Gluconeogenesis in liver. Cori-cycle. The hormonal regulation of gluconeogenesis. Storage
and mobilization of carbohydrates. Glycogenesis and glycogen breakdown. Pathological
aspects of glycogen metabolism. Regulation of blood sugar level. The effects of glucagon
and epinephrine on carbohydrate metabolism. Secretion and effects of insulin. Diabetes
mellitus. Synthesis of lactose in the mammary gland.
Lipid metabolism
The lipid composition of diet, medical importance. Storage and mobilization of fatty acids
from the adipose tissue. The oxidation of fatty acids, energetics and regulation. The
formation and utilization of ketone bodies. Physiological and pathological role of ketone
bodies. The synthesis of fatty acids, regulation of synthesis. The synthesis of phospholipids,
sphingolipids and glycolipids, pathological aspects. The synthesis of cholesterol, cholestryl
esters. Digestion and absorption of lipids in the gastrointestinal tract. Digestive enzymes.
The role of bile acids. Bile acid metabolism. The formation of gallstones. The transport of
lipids in the blood. Free fatty acids, lipoproteins. Chylomicron, VLDL metabolism. The
transport of cholesterol. LDL, HDL metabolism. LDL receptors. Hypercholesterolemias.
Biochemistry of atherosclerosis. Metabolism of steroid hormones. Synthesis, biological role
and catabolism of steroid hormones. Pathological aspects, enzymopathies. Eicosanoids.
Amino acid metabolism
Proteins as nutrients. Essential and nonessential amino acids. Digestion of proteins in the
gastrointestinal tract. Intracellular degradation of proteins. Transport of amino acids.
Glutathione metabolism. Synthesis of nonessential amino acids. Transamination. Breakdown
of amino acids with pathological aspects. Gluco- and ketoplastic amino acids. The fate of
ammonia. The ornithin cycle regulation, pathological aspects. Precursor functions of amino
acids. Synthesis and degradation of heme compounds. The bilirubin metabolism.
Metabolism of nucleotides
Digestion of DNA and RNA, absorption from the gastrointestinal tract. Purine nucleotides.
Synthesis of purines, salvage pathways. Synthesis of pyrimidine nucleotides. Formation of
deoxynucleotides. The breakdown of purines and pyrimidines. Formation of uric acid. Gout.
Biotransformation, metabolism of xenobiotics
Reactions of biotransformation, classification, characterization, regulation. Induction of
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 3
ccP450 isoenzymes. Inductive effects of drugs, environmental pollutants. The medical
importance of induction. The incomplete reduction of oxygen. Oxygen free radicals,
biomedical importance.
Metabolic interrelationships, the metabolism of individual tissues
Characteristics of intermediary metabolism of kidney, red blood cells and skeletal muscle.
The metabolic classification of skeletal muscles. The metabolism of adipose tissue,
hormonal effects on adipocytes. The intermediary metabolism of brain. Energy sources of
the brain. The role glucose. Interrelationship between glia-cells and neurons. Regulation of
metabolism on "key junctions": glucose-6-phosphate, pyruvate, fatty acyl-CoA. The
regulation of metabolism in the wellfed state. Interorgan relationships, regulation in the
liver. Regulation of metabolism in fasting. Interorgan relationships, regulation in the liver.
The biochemistry of short-term and the long-term fasting. Metabolic zonation in the liver.
The glucose paradox. The pathobiochemistry of diabetes mellitus.
Recommended books and handouts
Thomas M. Devlin: Textbook of Biochemistry with clinical correlations.
6th Edition including the on-line teaching system of WileyPlus Wiley-Liss, 2006.
Biochemistry Laboratory Manual Ed: Gy. Szabados (available on the website of the
department www.biokemia.sote.hu )
Biochemistry Consultation Manual (available on the website of the department
www.biokemia.sote.hu )
Students' own lecture notes
Schedule of the lectures
Monday
10:10-11:50 Hevesy György Lecture Hall Budapest IX., Tűzoltó utca 37-47. H-1094
Thursday 12:10-13:50 Hevesy György Lecture Hall Budapest IX., Tűzoltó utca 37-47. H-1094
Week MM,DD Topic
Lecturer
01
9,07
Intermediary metabolism, citric acid cycle, carbohydrate Dr. Miklós Csala
metabolism - overview
01
9,1O
Glycolysis
02
9,14
Metabolism of fructose and galactose. Gluconeogenesis. Dr. Miklós Csala
- habilitation lecture
02
9,17
Regulation of glycolysis and gluconeogenesis. Digestion Dr. Ágota Vér
of carbohydrates. - habilitation lecture
03
9,21
Metabolism of glycogen. Metabolism of disaccharides.
Metabolism of aminosugars
Prof. József Mandl
03
9,24
Pentose phosphate pathway, generation of NADPH.
Prof. József Mandl
04
9,28
Metabolism of lipids - overview. Absorption of lipids.
Prof. Veronika Ádám
04
10,01
Oxidation of fatty acids, ketone bodies.
Prof. Veronika Ádám
05
10,05
Synthesis of fatty acids.
Prof. Veronika Ádám
Dr. Miklós Csala
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 4
05
10,08
Lipoprotein metabolism.
Prof. Veronika Ádám
06
10,12
Phospholipid metabolism. Cholesterol metabolism and
transport.
Dr. Kraszimir Kolev
06
10,15
Pathobiochemistry of atherosclerosis
Dr. Kraszimir Kolev
07
10,19
Biosynthesis of steroid hormones
Prof. Miklós Tóth
1
07
10,22
Biosynthesis and biological role of eicosanoids
08
10,26
Degradation of proteins.
Dr. László Tretter
08
10,29
Biosynthesis of amino acids
Dr. László Tretter
09
11,02
Catabolism of amino acids I. Urea cycle
Dr. Katalin Bartha
09
11,05
Catabolism of amino acids II.
Dr. Katalin Bartha
10
11,09
Metabolism of nucleotides I.
Prof. Mária Sasvári
10
11,12
Metabolism of nucleotides II.
Prof. Mária Sasvári
11
11,16
Metabolism of porphyrins
Prof. Mária Sasvári
11
11,19
Biotransformation I.
Prof. József Mandl
12
11,23
Biotransformation II.
Prof. József Mandl
12
11,26
Integration of metabolism.
Dr. László Tretter
13
11,3O
Intermediary metabolism of tissues I.
Dr. László Tretter
13
12,03
Intermediary metabolism of tissues II.
Dr. László Tretter
14
12,07
Regulation of intermediary metabolism in fasting and in Dr. László Tretter
well-fed state I.
14
12,1O
Regulation of intermediary metabolism in fasting and in Dr. László Tretter
well-fed state II. Hormonal effects in the intermediary
metabolism.
Prof. Miklós Tóth
Schedule of practical lessons and seminars
Week Date
Topic
09.07.-09.11. Safety rules for work in the laboratory. & Amidolytic activity of trypsin.
1
09.14.-09.18. Enzyme kinetics – computer simulation
2
3
09.21.-09.25. Competitive inhibition of succinate dehydrogenase
4
09.28.-10.02. Lactic acidosis
5
10.05.-10.09. Oxidative phosphorylation in mitochondria
6
10.12.-10.16. Allosteric regulation of pyruvate kinase.
7
10.19.-10.22. Fructose intolerance, & McArdle's disease
8
10.26.-10.30. Digestion of lipids, role of bile acids
1 This lecture is held later, we publish its date and time on our homepage and we also send a neptun message Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 5
9
11.02.-11.06. Determination of serum cholesterol and triglyceride
10
11.09.-11.13. Lipoprotein lipase, & carnitine deficiency
11
11.16.-11.20.
12
11.23.-11.27 Metabolism of exercise
13
11.30.-12.04. Determination of serum transaminase and creatine kinase activities
14
12.07.-12.11.
Purification of trypsin by affinity chromatography. & Substrate specificity of
trypsin and chymotrypsin.
Hereditary hyperammonemias. & Vitamin B12 deficiency, methylmalonic
acidemia
Requirements
Practical lessons and seminars
The practical classes and the seminars are an essential part of the medical course in
biochemistry. Thus, the Department requires satisfactory attendance throughout the practical
course as a condition of the examination. If anybody has four or
more absences for whatever reason, we can not acknowledge their semester.
Grading of the performance of laboratory work
Lab work performance assessment is part of the semifinal exam. The practical work and its
documentation are assessed by the teachers at the end of each lesson. The lab performance is
graded by 1 point, if the measured results are well documented; the student’s records
demonstrate clearly the applied evaluation procedure and the conclusions from the
experiment. Otherwise the performance is graded by 0 points. The maximal total score of the
practical work for the semester is 8 points.
Midterm examination
Two midterm exams are held (5th and 12th week) for all classes (the FM course students can also
participate). (the 8th of October at 17:30-18:45 and 19:00-20:15; the 26th of November at 17:0018:15 and 18:30-19:40 at the Szent-Györgyi Albert Lecture Hall). (See details at the homepage
www.biokemia.sote.hu )
The midterm examinations are evaluated with grades from 1 up to 5 (excellent). The topics for the
1st midterm exam are those covered by the first 8 lectures (7. September – 1. October) as well as
the experiments and the seminars of the first 4 weeks, whereas for the second one - the questions
discussed in the lectures between 5th October and 20th November and the experiments and seminars
of weeks #6 through #11.
No opportunity for retake of failed midterm exams is given; students who are ill at the time of the
midterms can compensate the absence on the 3rd December (17:00-18:15) at the lecture hall Hevesy
György after presenting their medical certificate.
Semifinal examination
The grade of the semifinal exam is based on three elements:
1. theoretical written test;
2. practical exam;
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 6
3. bonus points collected in the course of the semester.
1. Theoretical written test:
The test consists of 60 questions of multiple choice type. The questions are based on the
recommended textbook, the lectures and the seminars. The questions are divided in two
blocks and further points are added to the score from each block on the basis of the
midterms performed during the fall semester of 2009-2010 year. (Students of FM course
may write the midterm exams in the fall semester of 2009-2010. Grade of midterm exams of
former semesters are not accepted): 5 points for midterm grade 5, 4 points for midterm grade
4, 3 points for midterm grade 3 and 2 points for midterm grade 2. (the points from the first
midterm are added to the first block. Students can pass the exam with minimal score 17 from
each of the blocks. (exception – see '1 point rule' below).
2. Practical exam:
There are two types of laboratory exam.
(I)A facultative practical exam is held on the 14th week, on the last lab-lesson. Answers for the
facultative practical exams are graded by 0,1 or 2 points. Only 1 and 2 points are accepted for the
semifinal examination.
(II)Practical exam as a part of the semifinal examination: Students get one question based on the
attached “List of practical questions” and answer it in written form (in 15 min). The answers are
graded by 0, 1 or 2 points. Students can not pass the semifinal exam with grade 0 from the practical
exam.
3. Bonus points:
(maximal number 7) can be collected in the course of the semester according to the following
scheme:
- from the grading of the experimental work (see above)
• 3 points, if the sum of the collected experimental points is at least 6
• 2 points, if the sum of the collected experimental points is at least 5
• 1 point, if the sum of the collected experimental points is at least 4
- from oral presentations on the seminars accompanied by electronic (Linux/OpenOffice or
MS Office) presentations or written summaries in electronic format, which are distributed
through the on-line teaching system (max. 4 bonus points in case of more presentations)
• 2 bonus points, if the student understands the content of the presented paper, emphasizes the
biochemical interrelations and interprets the presented article at the expected level of
knowledge
• 1 bonus point, if the student understands the content of the presented paper, but the
presentation can be followed only with substantial help on behalf of the teacher
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 7
Grades of the semifinal exam
Total score from the 3 elements of the semifinal
Grade
If both blocks contain 16 points or less in any of them, and/or practical exam
graded by 0*
1 (fail)
35-40
2 (pass)
41-48
3 (fair)
49-56
4 (good)
57-79
5 (excellent)
*If one block contains 16 and the other one 17 points and the practical exam is graded by
either 1 or two, grade for semifinal is 2 (pass) if the total scores are 41 points or higher.
Dates for semifinal exam
Two dates per week in the examination session are scheduled. Applications should be
submitted through the University administration system Neptun. Unsuccessful exams can be
repeated after 3 days.
Exemptions from semifinal and final exams
Those students who would like to be exempted from the biochemistry course on the basis of
their previous studies are kindly asked to present their documents to the teaching secretary.
The deadline of this application is 25th of September. Students with the proper academic
background are entitled to sit for a checking examination. In the case of successful
examination the exemption will be granted by the department. The date of exam can be fixed
by the teaching secretary and the most likely date will be on the fifth week (5.10-9.10.2009)
of the fall semester.
LIST OF TOPICS FOR THE SEMIFINAL EXAMS
Groups of questions:
Practical questions
Carbohydrate (metabolic integration)
Lipid (metabolic integration)
Amino acids-nucleotides
Please find enclosed the list of obligatory formulas as well.
PRACTICAL QUESTIONS
1. Competitive inhibition of succinate dehydrogenase by malonate
2. Mitochondrial oxidation I.: Experimental conditions for determination of oxygen
consumption by intact mitochondria. Definition and experimental measurement of P/O
ratio.
3. Mitochondrial oxidation II.: Please draw the curve of mitochondrial oxygen
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 8
4.
5.
6.
7.
8.
consumption after consecutive addition of glutamate/malate – ADP – atractylozide –
DNP – oligomycin – CN-. Explain the curves briefly.
Isoenzymes: pyruvate kinase
Digestion of lipids, determination of lipase activity
Measurement of blood plasma cholesterol and triacylglycerol
Purification of trypsin by affinity chromatography and substrate specificity of trypsin
and chymotrypsin
Determination of serum transaminase and creatine kinase activities
CARBOHYDRATES
1.Major carbohydrate components of food. Their digestion and absorption. Lactose intolerance.
2.GLUT family glucose transporters (localisation, special characteristics and role).
3.The pathway and importance of anaerobic glycolysis. Major lactate producing cells and tissues.
4.Glucose phosphorylation. Its role in the metabolism of the cell. The different regulation of the
isoenzymes.
5.Hormonal and allosteric regulation of glycolysis in the liver.
6.Energetics of aerobic and anaerobic glucose catabolism. Metabolic efficiency, participation of
oxidative and substrate-level phosphorylation.
7.Molecular mechanism and metabolic rationale of Pasteur-effect.
8.Which non-carbohydrate precursors can be converted to glucose, in which organs and how?
9.Compartmentation of gluconeogenesis. The glucose-6-phosphatase system and von Gierke's
disease.
10.Hormonal and allosteric regulation of gluconeogenesis in the liver.
11.The importance of the different regulation of pyruvate kinase isoenzymes in liver (PK-L) and
muscle (PK-M). Other points of coordinating the hepatic glycolysis and gluconeogenesis.
12.Hepatic metabolism of fructose. The regulatory/toxic effects of fructose-1-phosphate.
13.What is the fate of fructose in essential fructosuria? Metabolic consequences of fructose
intolerance. What is the pathomechanism of hypoglycemia and hyperuricemia in hereditary fructose
intolerance?
14.Entry of galactose into the glycolytic-gluconeogenetic pathway. Galactose intolerance.
15.UDP-galactose production from glucose in extrahepatic tissues. The role of UDP-galactose.
Localisation, structure and function of lactose synthase.
16.The oxidative branch of pentose-phosphate pathway. Its special role in the "biological oxidation"
and its regulation.
17.The non-oxidative branch of pentose-phosphate pathway. The co-operation of the two branches
in various conditions.
18.The mitochondrium-dependent and mitochondrium-independent NADPH2 production. The most
important NADPH2 consuming reactions. Drug-induced hemolytic anemia.
19.Aminosugar synthesis. Glycoproteins.
20.The pathway of glycogenesis from glucose. Glycogenin.
21.The pathway of glycogenolysis to glucose. Glycogen storage diseases.
22.Hormonal and allosteric regulation of hepatic glycogen metabolism.
23.Hormonal and allosteric regulation of glycogen metabolism in muscle.
24.Comparison of the glycogen metabolism of liver and muscle (function, regulation).
25.Role of key junctions in the regulation of metabolism. Glucose 6-phosphate.
26.Role of key junctions in the regulation of metabolism. Pyruvate.
27.The metabolism of red blood cells, muscle tissue and kidney.
28.Biochemistry of the resorptive /well fed/ state. a.) Metabolic interrelationship of tissues.
29.Biochemistry of the resorptive /well fed/ state. b.) Regulation of the main metabolic pathways in
Medical Biochemistry I. - Information-booklet 2009-2010 year fall semester 9
the liver.
30.Biochemistry of fasting. a,) Metabolic interrelationship of tissues.
31.Biochemistry of fasting. b.) Regulation of the main metabolic pathways in the liver.
32.The Cori cycle.
33.Regulation of the blood sugar level.
34.The effects of glucagon in the metabolism.
35.The metabolic effects of insulin.
36.The biochemistry of diabetes.
37.What is the mechanism of development of lactic acidosis in the absence of pyruvate
dehydrogenase activity? What further symptoms can be observed, if pyruvate dehydrogenase
deficiency is caused by the lack of lipoamide dehydrogenase subunit?
38.What is the mechanism of brain damage detected in pyruvate carboxylase deficiency? Explain
the development of hyperammonemia. Which metabolic pathways can be associated with the
pyruvate carboxylase function?
39.What is the effect of physical exercise on the lactate concentration of venous blood coming from
working muscles in normal subjects and in patients with McArdle's disease?
LIPIDS
1.Lipid-water interactions and their biological significance.
2.Digestion and absorption of lipids.
3.General rules of lipid transport. Structure and functions of major lipoprotein classes.
4.Chylomicrons. Composition, formation, catabolism. Role of lipoprotein lipase.
5.VLDL. Composition, formation, catabolism.
6.LDL . Composition, metabolic fate. It’s role in the transport of cholesterol. LDL receptors and
familial hypercholesterolemia (type II).
7.HDL. Composition, metabolic fate. It’s role in the transport of cholesterol.
8.Storage and mobilization of triacylglycerols. Regulation of both processes.
9.Transport of fatty acids through the inner mitochondrial membrane. Regulation of the transport.
10.Beta oxidation of saturated fatty acids. The energetics of oxidation. Regulation of beta oxidation
in the muscle and in the liver.
11.Oxidation of unsaturated fatty acids and fatty acids with odd number of carbon atoms.
12.Biosynthesis of saturated fatty acids.
13.Regulation of fatty acid synthesis.
14.Role of the adipose tissue in the carbohydrate and lipid metabolism.
15.Synthesis of mono- and polyunsaturated fatty acids. The essential fatty acids. Conversion of
linoleate to arachidonate.
16.Eicosanoids.
17.Synthesis and metabolic fate of ketone bodies. Regulation of synthesis.
18.The physiological role of ketone bodies.
19.Synthesis of cholesterol. Synthesis and importance of cholesterol esters.
20.Regulation of cholesterol synthesis.
21.Metabolism of the bile acids. Synthesis, regulation of synthesis, enterohepatic circulation.
Clinical aspects.
22.Biosynthesis of adrenal steroid hormones. Mineralocorticoid synthesis.
23.Biosynthesis of adrenal steroid hormones. Synthesis of glucocorticoid hormones.
24.Biosynthesis of androgen and estrogen hormones.
25.Biosynthesis, degradation and remodeling of phospholipids (phosphatidylcholine,
phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol, cardiolipine): reactions,
enzymes, intracellular localization.
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26.Regulatory mechanisms responsible for the maintenance of the appropriate cellular ratios of
phospholipids (regulation of the phosphatidylcholine biosynthesis). Structural requirements for the
diverse biological roles of the phospholipids. Pathological states related to abnormal phospholipid
metabolism (e.g. neonatal respiratory distress syndrome).
27.Metabolism of sphingolipids and glycolipids.
28.Role of key junctions in metabolism. Fatty acyl-CoA, metabolic fate, regulation.
29.Regulation of trigliceride and phospholipid metabolism in the liver.
30.The metabolism of brain. Metabolic properties of neurons and astrocytes.
31.Reverse cholesterol transport, biochemistry of atherosclerosis.
32.The role of carnitine. What forms and consequences of carnitine deficiency can be detected in
humans?
33.The function of lipoprotein lipase. How are lipoprotein lipase isoenzymes regulated in various
organs and in various physiological conditions?
AMINO ACID AND NUCLEOTIDE METABOLISM
1.Metabolism of proteins: nutritional requirements, deficiency states.
2.Degradation of proteins in the gastro-intestinal tract I. Endopeptidases /zymogens, activation,
substrate specificity/.
3.Degradation of proteins in the gastro-intestinal tract II. Exopeptidases and absorption of amino
acids.
4.L-glutamate dehydrogenase. The role of glutamic acid in the deamination of amino acids,
transdeamination.
5.The role of aspartate in the metabolism of N-containing compounds. Purine nucleotide cycle.
6.Transamination. Mechanism, metabolic importance, the role of pyridoxal phosphate.
7. The transport of ammonia, the role of glutamine and alanine. Glutamine synthesis and the loss of
the amide-group.
8.Urea cycle. Reactions, regulation, metabolic disorders.
9.Glucoplastic and ketoplastic amino acids: the metabolic intermediates produced from the carbon
skeletons of amino acids.
10.Amino acids forming pyruvate /mechanisms/.
11.Amino acids forming succinyl-CoA /mechanisms/.
12.Amino acids forming alpha-ketoglutarate and oxaloacetate /mechanisms/.
13.The catabolism of phenylalanine and tyrosine /main intermediates and enzyme defects/.
14.The role of methionine as a methyl group donor in biosynthetic reactions, the metabolism of
methionine, synthesis of polyamines.
15.The role of folate coenzymes in the metabolism.
16.The synthesis of nonessential amino acids: serine, cysteine aspartate, alanine, glutamate.
17.The "de novo" synthesis of ornithine and proline.
18.The metabolism of glycine. The synthesis of creatine.
19.The biosynthesis of heme, regulation of heme biosynthesis.
20.The catabolism of heme, formation and metabolism of bile pigments.
21.The catabolism of sulfur-containing amino acids. The formation and metabolic importance of
"active sulfate".
22.Cytoplasmic and mitochondrial synthesis of carbamoyl phosphate.
23.The sources of the constituent atoms of the purine ring. Synthesis and regulation of purine
nucleotides.
24.The structure and role of the active form of folic acid in the synthesis of nucleotides. The
synthesis of thymidilate. The molecular basis of the actions of the antimetabolites of folic acid.
25.The biosynthesis of pyrimidine nucleotides and its regulation in mammalian tissues.
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26.The biosynthesis and regulation of deoxyribonucleotides.
27.Salvage reactions in the metabolism of purine nucleotides.The Lesch-Nyhan syndrome.
28.The degradation of purine and pyrimidine nucleotides. Metabolic diseases in the catabolism of
purines.
29.Biotransformation: reactions of the first and second phase, biological significance, clinical
aspects.
30.Reactions and significance of cytochrome P450 isozymes.
31.Conjugation of xenobiotics and of endogenous substrates.
32.The pathogenesis and consequences of hyperammonemias
33.The effect of per os and parenteral administration of cyanocobalamin on the amino acid
metabolism.
FORMULAS
ATP, cAMP, CTP, GTP, IMP, TTP, orotate, urate, 1,3-diphosphoglycerate, 2phosphoglycerate, α-ketoglutarate, acetate, citrate, dihydroxiacetonephosphate, fumarate,
isocitrate,
malate, oxaloacetate, phosphoenolpyruvate, succinate
alanine, arginine, asparagine, aspartate, citrulline, cystein, glutamate, glutamine, glycine,
histidine, hydroxiproline, isoleucine, leucine, lysine, methionine, ornithine, phenylalanine,
proline, serine, threonine, tryptophan, tyrosine, valine, urea
α-amino-ß-ketoadipate, acetylcholine, carbamoyl-phosphate, creatine, creatine-phosphate,
creatinine, epinephrine, ethanolamine, γ-aminobutyrate, histamine, norepinephrine, Saminolevulinate, serotonine, ß-alanine, tryptamine
3-phosphoglycerate, 6-phosphogluconate, carnitine, fructose, fructose-1,6-bisphosphate, fructose6- phosphate, galactose, glucose, glucose-1-phosphate, glucose-6-phosphate, glucoseamine,
glucuronate, glyceraldehide-3- phosphate, ribose-5- phosphate, ß-hydroxi-ß-methylglutarate,
acetoacetate, ß-hydroxibutyrate
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