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Amino Acid Catabolism
Amino Acid Catabolism

... • Transfer of an amino group from an α-amino acid to an α-keto acid • In amino acid biosynthesis, the amino group of glutamate is transferred to various α-keto acids generating α-amino acids • In amino acid catabolism, transamination reactions generate glutamate or aspartate ...
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Biosynthesis of non-amino acids from amino acid precursors

...  Pool of glutamine in blood serves several functions  Provides ammonia for excretion of H in urine as NH4+  Fuel for gut, kidney, cells of immune  Source of N for rapidly dividng cells  Formation of glutamine from gluatamate and NH4+ provides a means of removing ammonia and transporting glutama ...
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... propagation and enhance proper cell metabolism. Still other media supplements may be added to create conditions which will elicit specific cellular responses and effects, such as altered protein biosynthesis, accelerated antibody production and secretion, toxic response mechanisms, etc. As a result, ...
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Fermentation and Biosynthetic Pathways File
Fermentation and Biosynthetic Pathways File

... carbon atoms required to synthesize glucose are derived from the intermediates produced during glycolysis, Krebs cycle and from lipids or amino acids. Bacteria may assemble it into the more complex polysaccharides. Biosynthesis of Lipids Lipids vary in chemical composition, cells synthesize fats by ...
Slide 1
Slide 1

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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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