Arginine amino acid synthesis

Moser et al. (1968) (one of the co-authors was Clifford Matthews) reported a peptide synthesis using the HCN trimer aminomalonitrile, after pre-treatment in the form of a mild hydrolysis. IR spectra showed the typical nitrile bands (2,200 cm ) and imino-keto bands (1,650 cm ). Acid hydrolysis gave only glycine, while alkaline cleavage of the polymer afforded other amino acids, such as arginine, aspartic acid, threonine etc. The formation of the polymer could have occurred according to the scheme shown in Fig. 4.9. 

More than a decade ago, it became clear that the human body makes NO. It is made in the brain, in the muscle cells which exist in the interior of the blood vessels, by macrophages (white cells that form an important part of the immune system), by the corpus cavemosum of the penis, and perhaps elsewhere. NO plays an important role in each of these tissues. The source of the atoms for the synthesis of NO is the common amino acid arginine (chapter 9). Under the influence of an enzyme termed NO synthase, arginine is converted to NO (and other products). The lifetime of NO in the tissues is quite short, a few seconds, but it lasts long enough to be effective. 

The non-essential amino acids are alanine, arginine, aspartate, asparagine, cysteine, glutamate, glutamine, glycine, proline, serine and tyrosine. A summary of the reactions involved in their synthesis is given in Figure 8.3 and full details of these pathways are provided in Appendix 8.2. 

The synthesis of arginine from citrulline. The latter is produced from other amino acids in the small intestine and then released into the blood. The kidney takes up citrulline and converts it to arginine, which is then released into the blood for use by other tissues (Figure 8.18). Since arginine is a precursor for a number of important compounds, and aids wound healing, this is a significant biochemical role of the kidney. 

They are required for the synthesis of conditionally essential amino acids, e.g. arginine, glycine, cysteine and glutamine. 

The anorexia suffered by cancer patients is likely to arise from a combination of psychological stress, altered senses of taste and smell and increased levels of cytokines, which influence the appetite and satiety centres in the hypothalamus. There are several consequences micronutrient intake will be diminished and this may contribute to the signs and symptoms of the disease. Plasma amino acid levels will fall, as in starvation (Chapter 16). Synthesis of glutamine (by muscle, adipose and lung), aspartate (by liver), glutathione (by the intestine) and arginine (by the kidney) will all be compromised. The metabolic significance of all of these is discussed in Chapter 18. 

In plants, this non-protein amino acid is derived from L-glutamate and in animals from L-arginine. Moreover, Figure 23 demonstrates that synthesis of alkaloids is complicated by the ability of the same amino acid to synthesize many different alkaloids. 

Humans have no dietary requirement for protein, per se, but, the protein in food does provide essential amino acids (see Figure 20.2, p. 260). Ten of the twenty amino acids needed for the synthesis of body proteins are essential—that is, they cannot be synthesized in humans at an adequate rate. Of these ten, eight are essential at all times, whereas two (arginine and histidine) are required only during periods of rapid tissue growth characteristic of childhood or recovery from illness. 

Figure 24-10 Biosynthesis of citrulline, arginine, and urea. The green arrows indicate reactions directly involved in deamination of amino acids and the synthesis of urea. N from amino acids and C from C02 are traced in green.

Glutamate serves as the starting material for the synthesis of glutamine, proline, and arginine (see fig. 21.1). Appropriately, these four amino acids are described as belonging to the glutamate family. In fungi, lysine is also included in this family (see fig. 21.1). 

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