Methionine essential amino acid

As constituents of proteins the amino-acids are important constituents of the food of animals. Certain amino-acids can be made in the body from ammonia and non-nitrogenous sources others can be made from other amino-acids, e.g. tyrosine from phenylalanine and cystine from methionine, but many are essential ingredients of the diet. The list of essential amino-acids depends partly on the species. See also peptides and proteins. 

Because of the simplicity of swiae and poultry feeds, most feed manufacturers add vitamins (qv) and trace minerals to ensure an adequate supply of essential nutrients. Amino acids (qv) such as methionine [7005-18-7] lysiae [56-87-17, threonine [36676-50-3] and tryptophan [6912-86-3], produced by chemical synthesis or by fermentation (qv), are used to fortify swiae and poultry diets. The use of these supplements to provide the essential amino acids permits diets with lower total cmde proteia coateat. 

The nutritional value of a proteia can be improved by the addition of amino acids of low abundance ia that proteia. Thus the fortification of plant proteias such as wheat, com, and soybean with L-lysiae, DL-methionine, or other essential amino acids (L-tryptophan and L-threonine) is expected to alleviate some food problems (11). Such fortification has been widespread ia the feedstuff of domestic animals. 

Currently available proteins are all deficient to greater or lesser extent in one or more of the essential amino acids. The recently advanced plastein reaction (229) has made it possible to use protein itself as substrate and to attach amino acid esters to the protein with high efficiency. By this method, soy bean protein (which is deficient in methionine) has been improved to the extent of having covalently attached L-methionine at 11%. 

In terms of amino acids bacterial protein is similar to fish protein. The yeast s protein is almost identical to soya protein fungal protein is lower than yeast protein. In addition, SCP is deficient in amino acids with a sulphur bridge, such as cystine, cysteine and methionine. SCP as a food may require supplements of cysteine and methionine whereas they have high levels of lysine vitamins and other amino acids. The vitamins of microorganisms are primarily of the B type. Vitamin B12 occurs mostly hi bacteria, whereas algae are usually rich in vitamin A. The most common vitamins in SCP are thiamine, riboflavin, niacin, pyridoxine, pantothenic acid, choline, folic acid, inositol, biotin, B12 and P-aminobenzoic acid. Table 14.4 shows the essential amino acid analysis of SCP compared with several sources of protein. 

Two amino acids—cysteine and tyrosine—can be synthesized in the body, but only from essential amino acid ptecutsots (cysteine from methionine and tyrosine from phenylalanine). The dietary intakes of cysteine and tytosine thus affect the requirements for methionine and phenylalanine. The remaining 11 amino acids in proteins are considered to be nonessential or dispensable, since they can be synthesized as long as there is enough total protein in the diet—ie, if one of these amino acids is omitted from the diet, nitrogen balance can stiU be maintained. Howevet, only three amino acids—alanine, aspartate, and glutamate—can be considered to be truly dispensable they ate synthesized from common metabolic intetmediates (pyruvate, ox-... 

Birds eat sufficient food to satisfy their energy intake, but this does not mean that they will eat enough protein, unless the protein proportion in the rotation is high. Protein quality is also important, the two most essential amino acids being lysine and methionine. The best quality protein for all poultry is white fishmeal (banned only for ruminants by the Soil Association). The best vegetable protein is soya bean which is low in methionine, but this can be made up by using sunflower meal in the ration. 

The grain or pulse forms of legumes have a high total protein content (20-26%) and can therefore be used as a natural supplement to cereals. Pulses are normally deficient in the essential amino acids methionine and cystine but contain enough lysine, whereas cereals are deficient in lysine but contain enough methionine and cystine. 

By the 1930s many workers had shown that nutritionally inadequate proteins, such as zein from maize, could be effective as a source of nitrogen if supplemented by additional amino acids (for zein, tryptophan). Even if it contained all the essential amino acids, the amount of protein in the diet influenced the results. Osbome and Mendel found that if the diet contained 18% by weight casein, which is low in cystine, young rats grew, but if the amount of protein was diminished, added cystine was required to offset the relative deficiency of this amino acid. Later, after methionine had been discovered, it was shown to replace the need for cystine. 

Humans have a limited capacity to synthesize amino acids de novo, but extensive interconversions can occur. Those amino acids which cannot be formed within the body and must be supplied by the diet are called essential . Members of this group, which includes the branched chain amino acids leucine and valine, and also methionine and phenylalanine, are all dietary requirements. Such essential amino acids may be chemically converted, mainly in the liver, into the non-essential amino acids. The term non-essential does not equate with not biochemically important but simply means they are not strict dietary components. 

Finally, they may be classified on the basis of whether they are nonessential, essential (exogenous), and conditionally essential amino acids. Food and tissue proteins contain 20 amino acids of nutritional importance. Nine of these amino acids (histidine (His), He, Leu, Lys, methionine (Met), Phe, Thr, Trp, and Val) cannot be synthesized by the body and they are therefore essential or indispensable nutrients that must be... 

Figure 8.3 A summary of pathways involved in the synthesis of non-essential amino acids. Glutamate is produced from ammonia and oxoglutarate. Glutamate is the source of nitrogen for synthesis of most of the amino acids. Cysteine and tyrosine are different because they require the essential amino acids (methionine and phenylyalanine) for their synthesis. These two amino acids are, therefore, conditionally essential, i.e. when there is not sufficient methionine or phenylyalanine for their synthesis, they are essential (Details are in Appendix 8.2).

In methylcobalamin, X is a methyl group. This compound functions as a coenzyme for several methyltransferases, and among other things is involved in the synthesis of methionine from homocysteine (see p. 418). However, in human metabolism, in which methionine is an essential amino acid, this reaction does not occur. 

The nutritional value of proteins (see p. 360) is decisively dependent on their essential amino acid content. Vegetable proteins—e.g., those from cereals—are low in lysine and methionine, while animal proteins contain all the amino acids in balanced proportions. As mentioned earlier, however, there are also plants that provide high-value protein. These include the soy bean, one of the plants that is supplied with NH3 by symbiotic N2 fixers (A). 

Proteins are essential components of the diet, as they provide essential amino acids that the human body is not capable of producing on its own (see the table). Some amino acids, including cysteine and histidine, are not absolutely essential, but promote growth in children. Some amino acids are able to substitute for each other in the diet. For example, humans can form tyrosine, which is actually essential, by hydroxylation from phenylalanine, and cysteine from methionine. 

Because of their unique biological functions, a significant and growing part of new drug discovery and development is focused on this class of biomolecules. Their biological functions are determined by the exact arrangement, or sequence of different amino acids in their makeup. There are 20 naturally occurring amino acids, 8 of which are essential amino acids, namely, l-isoleucine, L-leucine, L-lysine, L-methionine, L-phenylalanine, L-valine, l-threonine, and L-tryptophan. 

Sulfur amirro acids, methionirre arrd cysteine, are limiting in partially defatted flours prepared from heated and unheated morama beans, containing 0.4 g methionine/100 g flours and 0.1 g cysteine/100 g flours. The major amino acids in morama flours are glutamic acid, aspartic acid, as well as tyrosine. This is in agreement with amino acid composition of morama beans reported by various researchers (Bousquet, 1982 Bower et al., 1988 Dubois et al., 1995 Maruatona et al., 2010). Morama bean flours seem to be comparable in terms of essential amino acids composition to commercial soybean flours (Maruatona et al., 2010). 

Homocysteine (Hey) metabolism is closely linked to that of the essential amino acid methionine and thus plays a central role in several vital biological processes. Methionine itself is needed for protein synthesis and donates methyl groups for the synthesis of a broad range of vital methylated compounds. It is also a main source of sulphur and acts as the precursor for several other sulphur-containing amino acids such as cystathionine, cysteine and taurine. In addition, it donates the carbon skeleton for polyamine synthesis [1,2]. Hey is also important in the metabolism of folate and in the breakdown of choline. Hey levels are determined by its synthesis from methionine, which involves several enzymes, its remethylation to methionine and its breakdown by trans-sulphuration. 

Excessive heat can cause destruction of amino acid residues. The amino acid most susceptible to direct heat destruction is cystine. Although not an essential amino acid, cystine does have a sparing effect on the dietary requirement for methionine. As a result, cystine destruction can be nutritionally important. In addition, many vegetable proteins are limiting in the sulfur amino acids. Cystine destruction would be particularly harmful for these proteins. 

Methionine, threonine, lysine, isoleucine, valine, and leucine are essential amino acids. Their biosynthetic pathways are complex and interconnected (Fig. 22-15). 

FIGURE 22-15 Biosynthesis of six essential amino acids from oxalo-acetate and pyruvate in bacteria methionine, threonine, lysine, isoleucine, valine, and leucine. Here, and in other multistep pathways, the enzymes are listed in the key. Note that L,L-a,e-diaminopimelate, the product of step (HI), is symmetric. The carbons derived from pyruvate (and the amino group derived from glutamate) are not traced beyond this point, because subsequent reactions may place them at either end of the lysine molecule. 

Cysteine is synthesized by two consecutive reactions in which homocysteine combines with serine, forming cystathionine, which, in turn, is hydrolyzed to a-ketobutyrate and cysteine (see Figure 20.8). Homocysteine is derived from methionine as described on p. 262. Because methionine is an essential amino acid, cysteine synthesis can be sustained only if the dietary intake of methionine is adequate. 

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