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Amino acid synthesis
- 1. WELCOME PRESENTED BY, KIRAN DASANAL (PALB7319 )
- 2. TOPIC NAME • SYNTHESISOF AMINO ACIDS. 1. Reduction of N2 to NH4. 2. Transamination. 3. Synthesis of amino acids by metabolic precursors.
- 3. INTRODUCTION • Amino acidsare organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain(R group) specific to each amino acid.
- 4. CLASSIFICATION • Nonpolar/hydrophobic aminoacids glycine,alanine,valine,leucine,methionine,phenyalalanine, proline •polar/hydrophilic amino acids serine, cysteine, tyrosine, glutamicacid, asparaticacid, lysine,arginine • Sulphur containing amino acids Cystine, methionine, cysteine
- 5. Nutritionally essential amino acids Nutritionallynon-essential amino acids Arginine Alanine Histidine Asparagine Isoleucine Aspartic acid Leucine Cysteine Lysine Glutamic acid Methionine Glutamine Phenylalanine Glycine Threonine Proline Tryptophan Serine Valine Tyrosine List of essential and non essential amino acids
- 6. SYNTHESIS OF AMINOACIDS • Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds.
- 7. STEPS…. 1. Reduction ofN2 to NH4. 2. Transamination. 3. Synthesis of amino acids by metabolic precursors.
- 8. 1) REDUCTION OFN2 TO NH4 • It is the first step during synthesis of amino acids. • In which reduction of N2 TO NH4 takes place. • The conversion of nitrogen to ammonia is a reduction reaction which is exergonic in nature • Biological fixation of nitrogen is carried out by a highly conserved complex of proteins called nitrogenase complex.
- 10. 2) TRANSAMINATION Transamination,a chemical reaction that transfers an amino group to a ketoacid to form new amino acids. This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to nonessential amino acids (amino acids that can be synthesized de novo by the organism). Transamination in biochemistry is accomplished by enzymes called transaminases or aminotransferases.
- 11. FOR EXAMPLE α-ketoglutarate actsas the predominant amino-group acceptor and produces glutamate as the new amino acid. Aminoacid + α-ketoglutarate ↔ α-keto acid + Glutamate Glutamate's amino group, in turn, is transferred to oxaloacetate in a second transamination reaction yielding aspartate. Glutamate+ oxaloacetate ↔ α- ketoglutarate + aspartate
- 12. Aminotransfer reaction betweenan amino acid and an alpha-keto acid Keto acids (also called oxo acids or oxoacids) are organic compounds that contain a carboxylic acid group and a ketone group.
- 13. 3) SYNTHESIS OFAMINO ACIDS BY METABOLIC PRECURSORS • All the 20 protein amino acids are derived from intermediates in glycolysis, citric acid cycle or the pentose phosphate pathway Nitrogen enters these pathways by way of glutamate and glutamine. • It is believed that the pathways in higher plants and animals are similar, but comparatively less is known of the enzymes involved.
- 14. AN OVERVIEW OFAMINO ACID BIOSYNTHESIS
- 15. 3-phosphoglycerate Serine Cysteine Glycine Pyruvate Alanine Valine Leucine Ribose-5-phosphate Histidine α-ketoglutarate Glutamate Glutamine Proline Arginine Oxaloacetate Aspartate Asparagine Methionine Threonine Isoleucine Lysine Phosphoenolpyruvate and erythrose-4-phosphate Phenylalanine Tyrosine Tryptophan SYNTHESISOF AMINO ACIDS BY METABOLIC PRECURSORS
- 16. AMINO ACIDS CHEMICALSTRUCTURES
- 17. REFERENCES • Baldwin E: An Introduction to Comparative Biochemistry. 4th ed. Cambridge University Press, New York. 1964. • Bender DA: Amino Acid Metabolism. 2nd ed. Wiley- Interscience, New York, 1985. • Wikipedia
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