By Guoyao Wu
Content material: Discovery and Chemistry of Amino Acids Definition and Nomenclature of AA Discovery of AA Chemical homes of AA Protein Digestion and Absorption of Peptides and Amino Acids category and content material of Protein in Diets Definitions of Digestion and Absorption Protein Digestion and Absorption of Peptides and AA in Monogastric Animals Protein Digestion and Absorption of Peptides and AA in Ruminants Synthesis of Amino Acids Synthesis of AA in Tissues and Cells of Animals together with people normal Pathways for Synthesis of AA in Animal Cells particular Pathways for Synthesis of AA in Animal Cells Pathways for Synthesis of AA in Microorganisms Synthesis of D-AA in Animal Cells and micro organism Conversion of D-AA to l-AA in Animal Cells and micro organism Degradation of Amino Acids common features of AA Degradation in Animal Cells Pathways for Degradation of AA in Animal Cells Catabolism of D-AA in Animal Cells Catabolism of L-AA and D-AA in Microorganisms Synthesis and Catabolism of exact Nitrogenous ingredients from Amino Acids construction of Dipeptides which include Histidine or Its Methylated Derivatives Synthesis and Degradation of GSH construction of Gly-Pro-Hydroxyproline Synthesis and Catabolism of Polyamines Synthesis and usage of Creatine Synthesis and Catabolism of L-Carnitine Synthesis and Catabolism of Purine and Pyrimidine Nucleotides Heme Synthesis and Catabolism Synthesis and Catabolism of Histamine Synthesis and Catabolism of Catecholamines, Thyroid Hormones, and Melanin Synthesis and Catabolism of Serotonin and Melatonin Synthesis and Catabolism of D-Glucosamine and Glycosaminoglycans Conjugation items for Excretion Synthesis of Urea and Uric Acid Ammonia construction and Toxicity in Animals Urea construction in Mammals Uric Acid Synthesis Comparisons among Uric Acid and Urea Synthesis Use of Isotopes for learning Amino Acid Metabolism simple techniques approximately Isotopes Interpretation of information from Isotope Experiments power Pitfalls of Isotopic stories Protein Synthesis historic views of Protein Synthesis Pathway Pathways of Protein Synthesis within the Cytoplasm and Mitochondria Biochemical features and value of Protein Synthesis Measurements of Protein Synthesis Intracellular Protein Degradation historic views of Intracellular Protein Degradation Proteases (Peptidases) for Intracellular Protein Degradation Intracellular Proteolytic Pathways features and Physiological value of Intracellular Protein Degradation Measurements of Intracellular Protein Degradation law of Amino Acid Metabolism simple strategies in Metabolism results of dietary and Physiological components on AA Metabolism Physiological capabilities of Amino Acids Roles of AA in Peptide Synthesis Roles of AA for Synthesis of Nonpeptide Molecules Regulatory Roles of AA in meals consumption, Nutrient Metabolism, and Gene Expression Roles for AA within the Immune reaction Use of AA in nutrients, remedy, and future health Efficacy and security of nutritional AA Supplementation Inborn blunders of Amino Acid Metabolism Inherited ailments because of problems of AA Metabolism therapy of Inborn error of AA Metabolism nutritional specifications of Amino Acids ancient views of nutritional AA necessities choice of AA necessities review of nutritional Protein caliber Index
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Additional resources for Amino acids : biochemistry and nutrition
Von Liebig in 1849. Such a reaction also occurs when AA are treated with sodium hypochlorite or chloramine-T. The formation of the aldehyde is specific to the AA under consideration, whereas ammonia and CO2 are generated nonspecifically from all AA. Another well-utilized oxidative deamination (decarboxylation) of an AA is its reaction with ninhydrin to yield colored products. This chemical reaction was discovered by S. Ruhemann in 1911 and its chemistry is very complex. First, an AA reacts with ninhydrin to form an intermediate amine, the corresponding aldehyde, carbon dioxide, and ammonia.
In 1846, another Austrian chemist, J. Redtenbacher, recognized the presence of sulfur in the taurine molecule and correctly identified its formula to be C2H7NO3S. The structure of taurine was established through chemical synthesis of ethylene dibromide, potassium thiocyanate, and ammonia by H. Kolbe in 1862. By the 1910s, taurine was known to be widely distributed in the animal kingdom and to be present in relatively high concentrations in all mammalian tissues. This AA has no asymmetric carbon and, therefore, has no isomer.
Leuchs in 1905. Subsequently, 4-hydroxy-l-proline was found to be an abundant constituent of collagen and elastin. Studies in the 1960s revealed that 4-hydroxy-l-proline is derived from the posttranslational hydroxylation of l-proline in proteins (primarily collagen) in the presence of oxygen, ascorbic acid, α-ketoglutarate, and Fe2+. l-Isoleucine (α-amino-β-methylvaleric acid) was one of the three branched-chain AA (BCAA) abundant in both plant proteins and most animal proteins but was the last BCAA to be discovered.