Methionine acid

Poly(irainocarbonyl-L-raethylthiopropylidene), [Poly(L-methionine)] acid (1/1, mol) ... 

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. 

M.p. 283 C (decomp.). Soluble in water and alcohol. The naturally occurring substance is laevorotatory. Methionine is one of the natural sulphur-containing amino-acids, and is present in small quantities in the hydrolysis pro-... 

When exposed to sunlight, it is converted to a white insoluble resin, disacryl. Oxidized by air to propenoic acid small amounts of hy-droquinone will inhibit this. Bromine forms a dibromide which is converted by barium hydroxide into DL-fructose. The acrid odour of burning fats is due to traces of propenal. It is used in the production of methionine and in controlled polymerization reactions to give acrolein polymers. ... 

In addition to codons for ammo acids there are start and stop codons Protein biosynthesis begins at a start codon and ends at a stop codon of mRNA The start codon IS the nucleotide triplet AUG which is also the codon for methionine The stop codons are UAA UAG and UGA... 

FIGURE 28 12 Translation of mRNA to an ammo acid sequence of a protein starts at an mRNA codon for methionine Nucleophilic acyl substitution transfers the N formylmethionme residue from Its tRNA to the ammo group of the next ammo acid (shown here as alanine) The process converts an ester to an amide... 

Section 28 12 The start codon for protein biosynthesis is AUG which is the same as the codon for methionine Thus all proteins initially have methionine as their N terminal ammo acid but lose it subsequent to their formation The reaction responsible for extending the protein chain is nucleophilic acyl substitution... 

The amino acid transferred to methionine is senne instead of alanine The senne tRNA sequence that is complementary to the UCU sequence of mRNA is AGA... 

The significance of industrial acrolein production may be clearer if one considers the two major uses of acrolein—direct oxidation to acryUc acid and reaction to produce methionine via 3-methyhnercaptopropionaldehyde. In acryUc acid production, acrolein is not isolated from the intermediate production stream. The 1990 acryUc acid production demand in the United States alone accounted for more than 450,000 t/yr (28), with worldwide capacity approaching 1,470,000 t/yr (29). Approximately 0.75 kg of acrolein is required to produce one kilogram of acryUc acid. The methionine production process involves the reaction of acrolein with methyl mercaptan. Worldwide methionine production was estimated at about 170,000 t/yr in 1990 (30). (See Acrylic ACID AND DERIVATIVES AmINO ACIDS, SURVEY.)... 

Methylmercaptopropionaldehyde is also used to make the methionine hydroxy analog CH2SCH2CH2CH(OH)COOH [583-91 -5] which is used commercially as an effective source of methionine activity (71). AH commercial syntheses of methionine and methionine hydroxy analog are based on the use of acrolein as a raw material. More than 170,000 tons of this amino acid are produced yearly (30) (see Amino acids). One method for the preparation of methionine from acrolein via 3-methyhnercaptopropionaldehyde is as follows. 

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. 

Sulfur deficiency usually is not a problem for mminants because the mminal microflora can utilize sulfur-containing amino acids. A deficiency can occur, however, when an NPN source is fed. L-Methionine [63-68-3] is the most biologically available source of sulfur (21). Various sulfates are intermediate in sulfur avadabiHty, and elemental sulfur is the least available source of sulfur. 

Not many fine chemicals have a production value exceeding 10 million per year. Less than a do2en achieve production volumes above 10,000 metric tons per year and sales of > 100 million per year. Apart from the pharmaceutical and pesticide fine chemicals these comprise the amino acids (qv), L-lysine and n,T-methionine used as feed additives (see Feeds AND FEED ADDITIVES), and vitamins ascorbic acid and nicotinic acid. 

Tables 2, 3, and 4 hst compositional and nutritional data of selected algae. Mote extensive compilations on algae ate available (26,58). Algae tend to have lower contents of methionine than is deskable in human and animal nutrition and supplementation with this amino acid is necessary with many species (Table 4).

Most of the bacteria, yeasts, molds, and higher fungi of interest for SCP production are deficient in methionine and must be supplemented with this amino acid to be suitable for animal feeding or human food appHcations. Also, lysine—arginine ratios should be adjusted in poultry rations in which yeast SCP is used (62). Human feeding studies have shown that only limited quantities of yeast such as Candida utilis can be added to food products without adverse effects on flavor (63). 

LPC Product Quality. Table 10 gives approximate analyses of several LPC products. Amino acid analyses of LPC products have been pubhshed including those from alfalfa, wheat leaf, barley, and lupin (101) soybean, sugar beet, and tobacco (102) Pro-Xan LPC products (100,103) and for a variety of other crop plants (104,105). The composition of LPCs varies widely depending on the raw materials and processes used. Amino acid profiles are generally satisfactory except for low sulfur amino acid contents, ie, cystine and methionine. 

The sulfur amino acid content of soy protein can be enhanced by preparing plasteins from soy protein hydrolysate and sources of methionine or cystine, such as ovalbumin hydrolysate (plastein AB), wool keratin hydrolysate (plastein AC), or L-methionine ethyl ester [3082-77-7] (alkaU saponified plastein) (153). Typical PER values for a 1 2 mixture of plastein AC and soybean, and a 1 3 mixture of alkah-saponified plastein and soybean protein, were 2.86 and 3.38, respectively, as compared with 1.28 for the soy protein hydrolysate and 2.40 for casein. 

Enzymatic hydrolysis is also used for the preparation of L-amino acids. Racemic D- and L-amino acids and their acyl-derivatives obtained chemically can be resolved enzymatically to yield their natural L-forms. Aminoacylases such as that from Pispergillus OTj e specifically hydrolyze L-enantiomers of acyl-DL-amino acids. The resulting L-amino acid can be separated readily from the unchanged acyl-D form which is racemized and subjected to further hydrolysis. Several L-amino acids, eg, methionine [63-68-3], phenylalanine [63-91-2], tryptophan [73-22-3], and valine [72-18-4] have been manufactured by this process in Japan and production costs have been reduced by 40% through the appHcation of immobilized cell technology (75). Cyclohexane chloride, which is a by-product in nylon manufacture, is chemically converted to DL-amino-S-caprolactam [105-60-2] (23) which is resolved and/or racemized to (24)... 

Sulfur. Sulfur is present in every cell in the body, primarily in proteins containing the amino acids methionine, cystine, and cysteine. Inorganic sulfates and sulfides occur in small amounts relative to total body sulfur, but the compounds that contain them are important to metaboHsm (45,46). Sulfur intake is thought to be adequate if protein intake is adequate and sulfur deficiency has not been reported. Common food sources rich in sulfur are Hsted in Table 6. 

Calculated as sulfur-containing amino acids, methionine plus cystine. Serving corresponds to 236 mL (1 cup) unless otherwise noted. Serving corresponds to 113 g (4 oz). 

Evidence soon emerged that the endogenous opioids were peptides rather than simple morphine-like molecules (9). The first direct evidence for endogenous opioids in brain extracts was provided in 1975 when two pentapeptides were purified that differed only in the carboxyl terminal amino acids (10) (Table 1). These peptides were called methionine- (Met-) and leucine- (Leu-) enkephalin, from the Greek term meaning "in the head."... 

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