Cystine ammonia

It has been shown that the presence of chloride ion (hydrochloride salts of aminothiols are often used) in addic solution decreases S—S cleavage and increases ammonia yields with cystine . (Ammonia is a major product of both e q and OH attack on amino acids and peptides not having thiol or disulphide groups. )... 

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. 

Tyrosine and cystine are colourless solids almost insoluble in water gfid in ethanol (tyrosine dissolves in hot water). They are readily soluble in dilute caustic alkali solution, in ammonia and mineral acids, but not in acetic acid. They are also classed as neutral ampholytes. ... 

Niiroprusside test. Dissolve about o-i g. of cystine in a few ml. of dilute ammonia and then add a few drops of potassium cyanide solution. This reduces cystine to cysteine,... 

Dialkyl esters of cystine (39) and lanthionine (40) undergo a surprising thermolysis reaction at between 25 C and 80 °C to afford cis and trans methyl 2-methylthiazolidine-2,4-dicarboxylates (43) in protic solvents. A two stage process is proposed for this transformation. An initial i-elimination reaction gives the thiol (41) and the enamine (42). Thiol addition to the imine tautomer of (42) is then followed by loss of ammonia and an intramolecular cyclisation to give (43) <96CC843>. 

Hyperargininemia. This defect is characterized by elevated blood and cerebrospinal fluid arginine levels, low erythrocyte levels of arginase (reaction 5, Figure 29-9), and a urinary amino acid pattern resembling that of lysine-cystinuria. This pattern may reflect competition by arginine with lysine and cystine for reabsorption in the renal tubule. A low-protein diet lowers plasma ammonia levels and abolishes lysine-cystinuria. 

Electrosynthesis Co. Inc. [109,112, 113] has piloted a process that reduces cystine in aqueous ammonia solution, using an ElectroSyn cell. 

The oxidation of cysteine, as well as other amino acids, was studied by Mudd et a/. Individual amino acids in aqueous solution were exposed to ozone the reported order of susceptibility was cysteine, methionine, tryptophan, tyrosine, histidine, cystine, and phenylalanine. Other amino acids were not affected. This order is similar to that for the relative susceptibility of amino acrids to radiation and to lipid peroxides. Evaluation of the ozonization products revealed that cysteine was converted to cysteic acid, as well as cystine methionine to methionine sulfoxide tryptophan to a variety of pioducrts, including kynurenine and N-formylkynurenine tyrosine also to a variety of products, includiitg dihydroxyphenylalanine histidine to ammonia, proline, and other compounds and cystine in part to cysteic acid. In some cases, the rate and end products depended on the pH of the solution. 

There are two reports describing the preparation of derivatives of 1,2-thiazetidine-1,1-dioxide. The sulfur atom in L-cystine diethyl ester was oxidized and the corresponding sulfonyl chloride was cyclized with ammonia (Scheme 3) (60CB784). A similar transformation used protected )3-homocysteine as starting material (94LA251). 

L-Perhydro-l,4-thiazine-3-carboxylic acid 1-oxide is a natural AA found in some red and brown algae. It was synthesized from L-cystine in several steps. The heterocyclic ring was prepared by cyclization of 5-(2-chloro- or bromoethyl)-L-Cys in the presence of triethylamine. Perhydro-l,4-thiazine-3-carboxylic acid was then oxidized with H2O2/ACOH to give the sulfoxide (64JOC2203). Cystine also reacted with ethyl a-bromopropionate in liquid ammonia to give 5-oxoperhydro-l,4-thiazine-3-carboxylic acid [76JCS(P2)203],... 

This pyridoxal-phosphate-dependent enzyme [EC 4.4.1.8], also referred to as /3-cystathionase and cystine lyase, catalyzes the hydrolysis of cystathionine to yield homocysteine, pyruvate, and ammonia. 

The separation of cystine and tyrosine as they are obtained by hydrolysis with hydrochloric acid was described by Morner in I901. The protein—hair, keratin from horn, eggshells, etc.—was boiled with five times its quantity of 13 per cent hydrochloric acid under a reflux condenser on a water bath for six to seven days. The solution was then decolorised with charcoal and evaporated in vacuo, and the residue dissolved in 60 to 70 per cent, alcohol. The two acids then crystallised out on neutralising with soda, and were separated by fractional crystallisation from ammonia if much tyrosine was present it separated out first, but if cystine exceeded tyrosine in quantity this compound crystallised out first the remainder was only separated with difficulty. Embden separated the mixture of the two acids by means of very dilute nitric acid, in which tyrosine is very easily soluble, but cystine with difficulty. Their separation may also be effected by precipitation with mercuric sulphate in 5 per cent, sulphuric acid solution in which the mercury compound of tyrosine is soluble (Hopkins and Cole). 

Hoppe-Seyler, as cited by Baumann and Preusse, showed that the nitrogen of cystine was separated off as ammonia by alkalies and not as methylamine, as would be expected from this formula, and moreover maintained that the formula was C3H7NSO3. 

Fischer and Suzuki soon afterwards showed that Neuberg and Mayer s stone cystine contained tyrosine, and that its different behaviour to protein cystine was due to the presence of this compound. Rothera also could find no difference between stone cystine and protein cystine, and further, Gabriel s synthesis of isocysteine or a-thio-/8-aminopropionic acid and isocystine, which had quite different properties to cystine, though the two were much alike in many of their reactions, proved that stone cystine and protein cystine must be identical substances. Finally, it has been shown by Friedmann that a-thiolactic acid, ammonia PT. I. 4... 

Fig. 2.1.2a-c A Urine amino acids in a patient with cystinuria assayed by an amino acid analyzer (AAA). The indicated peaks are 1 glycine, 2 cystine, 3 ammonia, 4 ornithine, 5 lysine, 6 arginine, i.s. internal standard (S-amino thyl-cysteine). Cystinuria treatment is best followed-up by analyzing an early morning urine specimen, which usually shows the highest amino acid concentrations. b-c see next page... 

L-Cystine [56-89-3] M 240.3, [oc]d -229° (c 0.92 in M HCI). Cystine disulphoxide was removed by treating an aqueous suspension with H2S. The cystine was filtered off, washed with distilled water and dried at 100° under vacuum over P2O5. Crystd by dissolving in 1.5M HCI, then adjusting to neutral pH with ammonia. Likely impurities are D-cystine, meso-cystine and tyrosine. 

Thiocysteine can also arise in a similar manner through action of cystathionine (3 lyase on cystine. Thiocysteine is eliminated with production of pyruvate and ammonia from the rest of the cystine molecule 467 One of the nifS-like proteins of E. coli is thought to transfer a selenium atom from selenocysteine (pp. 823-827) into selenophosphate 466a f The latter can be formed by transfer of a phospho group from ATP to selenide HSe-. The other products of ATP cleavage are AMP and P . Reduction of Se° to HSe- is presumably necessary. 

For glutamic acid (18) and glycine (10) the yield of ammonia varies approximately as the cube root of the concentration. This variation agrees with the diffusion of the spur model which derives from the hypothesis that at higher solute concentrations, water radicals are scavenged which would react with each other in more dilute solution. However, for the effect of cathode rays on the aromatic amino acids phenylalanine, tryptophan, and tyrosine and for cystine, this relationship is inverted, and amino acid destruction decreased with an increase in concentration (29). 

A variant of this procedure is provided by the preparation of S-benzyl-l-cysteine (Expt 5.206). The required thiolate salt is prepared by the reductive cleavage with sodium in liquid ammonia of the disulphide linkage in the amino acid, (S)-cystine, and is alkylated in situ with benzyl chloride. The preparation of this S-benzyl derivative constitutes a method of protection of the thiol grouping in cysteine. 

A maltol-ammonia browning reaction produced thirteen pyrazines, two pyrroles, two oxazoles, and one pyridine (12). The major products of this system were 2-ethyl-3-hydroxy-6-methylpyridine and 2-ethyl-3,6-dimethylpyrazine. It is difficult to construct possible formation mechanisms for these compounds from maltol and ammonia. All the carbon atoms must come from maltol. It is possible, then, that maltol degrades into smaller carbon units and that these fragments recombine to form larger carbon units, producing these compounds. Recently, the formation of thiophenones and thiophenes from the reaction of 2,5-dimethyl-4-hydroxy-3(2H)-furanone and cysteine or cystine was reported (13. 14). All these reaction mixtures were reported to possess a cooked meat-like flavor. 

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