Download PRACTICAL LESSON 4 METABOLIC PATHWAY OF AMINO ACIDS

PRACTICAL LESSON 4
METABOLIC PATHWAY OF AMINO ACIDS
FINAL CONTROL
The purpose of the lesson:
- to obtain the knowledge about metabolic pathway of amino acids
Content of the lesson:
1. Programmed control.
2. Written control and discussion.
3. Decision of situation tasks.
QUESTIONS FOR PREPARATION FOR THE LESSON:
1. Functions of the protein in organism.
2. Stages of protein metabolism.
3. Essential, non-essential, semi-essential amino acids.
4. Nitrogen metabolism. Amino acids pool.
5. Protein turnover. Protein degradation.
6. Nitrogen balance.
7. Nutritional indices. Biological value of protein. Net protein utilization. Protein
efficiency ratio. Chemical score.
8. General characteristics of proteases. Endopeptidases, exopeptidases.
9. Digestion in stomach, duodenum, small intestine. Specificity of enzymes.
10. Absorption of free amino acids.
11. Hartnup’s disease. Cystinuria.
12. Putrefaction of amino acids. Detoxification of toxic products.
13. Putrefaction of tryptophan. Detoxification of indole.
14. Common fates of amino acids.
15. Conversion of α- amino group. Transamination.
16. Biological significance of ALT and AST.
17. Deamination for D- and L- amino acids. Oxidative deamination of glutamic
acid. Biological significance.
18. Transdeamination. Scheme. Biological significance.
19. Disposal of ammonia from tissues. Transport forms for ammonia.
20. Glucose- alanine cycle. Biological significance.
21. Mechanism of toxic action of ammonia and detoxification of ammonia in the
nervous tissue.
22. Urea cycle. Regulation, biological significance, disorders of urea cycle.
23. Ammoniogenesis in kidney. Biological significance.
24. Reactions decarboxylation of α- carboxyl group. General characteristic of
biogenic amines.
25. Biosynthesis of GABA, serotonin, histamine, dopamine in details. Biological
significance.
26. Fate of carbon skeletons. Glycogenic, ketogenic and glycoketogenic amino
acids.
27.
28.
29.
30.
31.
Metabolic fate of phenylalanine. Phenylketonuria.
Metabolic fate of tyrosine. Biosynthesis of catecholamines. Parkinsonism.
Biosynthesis of melanin. Albinism.
Catabolism of tyrosine in liver. Alcaptonuria.
Metabolic fate of methionine. Biological significance of transmethylation
reactions.
32. Biosynthesis of carnitine, phosphotidylcholine, adrenaline.
33. Synthesis of creatine. Biological significance of creatine phosphate.
34. Fate of branched-chain amino acids. Maple syrup urine disease.
TEST CONTROL
See Practical Lessons 1-3
RECOMMENDED BIBLIOGRAPHY
a) Compulsory:
1. Lectures.
2. DM Vasudevan, Sreekumari S, Kannan Vaidyanathan. (2014) Textbook of
biochemistry for medical students.7th edn. Jaypee Brothers Medical Publishers (P)
Ltd.
3. Robert K. Murray, David A Bender, Kathleen M. Botham, Peter J. Kennelly,
Victor W. Rodwell, P. Anthony Weil. (2009) Harper's Illustrated Biochemistry. 28th
edn. The McGraw-Hill Companies, Inc.
b) Supplementary:
1. Janice Gorzynski Smith. (2012) Principles of general, organic, and biological
chemistry. The McGraw-Hill Companies, Inc.
2. Laurence A. Moran, H. Robert Horton, K. Gray Scrimgeour, Marc D. Perry.
(2012) Principles of Biochemistry. Pearson Education, Inc.
3. Lehninger A., David L. Nelson, Michael M. Cox. (2008) Lehninger Principles of
Biochemistry. 5th edn. W.H.Freeman and company, New York.
4. Mary K. Campbell, Shawn O. Farrell Biochemistry. (2012) Biochemistry. 7th edn.
Brooks/Cole, Cengage Learning.
5. Pamela C. Champe, Richard A. Harvey, Denise R. Ferrier. (2004) Lippincott’s
Illustrated Reviews: Biochemistry. Lippincott Williams & Wilkins
6. Reginald H. Garrett, Charles M. Grisham. (2010) Biochemistry. Brooks/Cole,
Cengage Learning.