Amino acids, sulfur-containing

Methionine and cysteine are the principal sources of organic sulfur in humans. Methionine is essential (unless adequate homocysteine and a source of methyl groups are available), but cysteine is not, since it can be synthesized from methionine. 

Selected methyl transfer reactions involving S-adenosylmethionine. 

Homocysteine can be recycled back to methionine either by transfer of a methyl group from betaine catalyzed by betaine-homocysteine methyltransferase, or from N -methyltetrahydrofolate(N -methyl-FH4)catalyzedbyN -methyl-FH4-methyltransferase, which requires methyl cobalamin  

Methionine is utilized primarily in protein synthesis, providing sulfur for cysteine synthesis, and is the body s principal methyl donor. In methylation reactions, S-adenosylmethionine (SAM) is the methyl group donor. SAM is a sulfonium compound whose adenosyl moiety is derived from ATP as follows  

Betaine (an acid) is obtained from oxidation of choline (an alcohol) in two steps  

While sulfur-free amino acids are broken down to amines via decarboxylation, the sulfur-containing amino acids such as cysteine can undergo more complex reactions. Fisher and Scott suggest that, because cysteine produces a powerful reducing aminoketone, hydrogen sulfide could be produced by reducing mercaptoacetaldehyde or cysteine.2 

Ketose Sugar N-Fructosylamine (if ketose is fructose) Enol 2-Amino-l-Keto Sugar 

Alternatively, hydrogen sulfide could be produced alongside ammonia and acetaldehyde by the breakdown of the mercaptoimino-enol intermediate of the decarboxylation reaction of the cysteine-dicarbonyl condensation product. Fisher also points out that hydrogen sulfide is forms many odiferous an hence intensely flavoured products.2 Cysteine is important as it is one of the major sources of sulfur. 

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Since dietary cereals are low in sulfur-containing amino acids, they produce an alkaline urine which favors the retention of bone minerals. In post-menopausal women, there appears to be some interaction between the diet and the effect produced by estrogens on bone mineral content (28). 

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. 

Gelatin can be a source of essential amino acids when used as a diet supplement and therapeutic agent. As such, it has been widely used in muscular disorders, peptic ulcers, and infant feeding, and to spur nail growth. Gelatin is not a complete protein for mammalian nutrition, however, since it is lacking in the essential amino acid tryptophan [73-22-3] and is deficient in sulfur-containing amino acids. 

The differences in the amino acid chemistry of the hide coUagen and the hair keratin are the basis of the lime-sulfide unhairing system. Hair contains the amino acid cystine. This sulfur-containing amino acid cross-links the polypeptide chains of mature hair proteins. In modem production of bovine leathers the quantity of sulfide, as Na2S or NaSH, is normally 2—4% based on the weight of the hides. The lime is essentially an unhmited supply of alkah buffered to pH 12—12.5. The sulfide breaks the polypeptide S—S cross-links by reduction. Unhairing without sulfide may take several days or weeks. The keratin can be easily hydrolyzed once there is a breakdown in the hair fiber stmcture and the hair can be removed mechanically. The coUagen hydrolysis is not affected by the presence of the sulfides (1—4,7). 

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). 

Sulfoxides occur widely in small concentrations in plant and animal tissues, eg, aHyl vinyl sulfoxide [81898-53-5] in garlic oil and 2,2 -sulfinylbisethanol [3085-45-8] as fatty esters in the adrenal cortex (1,2). Homologous methyl sulfinyl alkyl isothiocyanates, which are represented by the formula CH3SO(CH2) NCS, where n = 3 [37791-20-1], 4 [4478-93-7], 5 [646-23-1], 8 [75272-81-0], 9 [39036-83-4], or 10 [39036-84-5], have been isolated from a number of mustard oils in which they occur as glucosides (3). Two methylsulfinyl amino acids have also been reported methionine sulfoxide [454-41-1] from cockroaches and the sulfoxide of i -methylcysteine, 3-(methylsulfinyl)alaiiine [4740-94-7]. The latter is the dominant sulfur-containing amino acid in turnips and may account in part for their characteristic odor (4). 

The side groups of the amino acids vary markedly in size and chemical nature and play an important role in the chemical reactions of the fiber. For example, the basic groups (hisidine, arginine, and lysine) can attract acid (anionic) dyes, and in addition the side chains of lysine and hisidine are important sites for the attachment of reactive dyes. The sulfur-containing amino acid cysteine plays a very important role, because almost all of the cysteine residues in the fiber are linked in pairs to form cystine residues, which provide a disulfide bridge —S—S— between different polypeptide molecules or between segments of the same molecules as shown ... 

Potential consumer benefits from biotechnology (56) are cost and quaUty. The use of biotech means to increase the level of various sulfur-containing amino acids in coffee proteins, and to enhance sucrose and oil levels, could have an impact on the flavor and aroma of the finished ground coffee product. Also, caffeine level modification/elimination through genetic manipulations of the coffee plant could yield low caffeine coffee without additional processing by the manufacturer. 

The Dim ester was developed for the protection of the carboxyl function during peptide synthesis. It is prepared by transesterification of amino acid methyl esters with 2-(hydroxymethyl)-l,3-dithiane and Al(/-PrO)3 (reflux, 4 h, 75°, 12 torr, 75% yield). It is removed by oxidation [H2O2, (NH4)2Mo04 pH 8, H2O, 60 min, 83% yield]. Since it must be removed by oxidation it is not compatible with.sulfur-containing amino acids such as cysteine and methionine. Its suitability for other, easily oxidized amino acids (e.g., tyrosine and tryptophan) must also be questioned. It is stable to CF3CO2H and HCl/ether. - ... 

The nonpolar amino acids (Figure 4.3a) include all those with alkyl chain R groups (alanine, valine, leucine, and isoleucine), as well as proline (with its unusual cyclic structure), methionine (one of the two sulfur-containing amino acids), and two aromatic amino acids, phenylalanine and tryptophan. Tryptophan is sometimes considered a borderline member of this group because it can interact favorably with water via the N-H moiety of the indole ring. Proline, strictly speaking, is not an amino acid but rather an a-imino acid. 

Mammalian sulfite oxidase is the last enzyme in the pathway for degradation of sulfur-containing amino acids. Sulfite oxidase (SO) catalyzes the oxidation of sulfite (SO ) to sulfate (S04 ), using the heme-containing protein, cytochrome c, as electron acceptor ... 

Thiols, thioethers and sulfoxides [37-39] e.g. sulfur-containing amino acids... 

Cooper AJL Biochemistry of the sulfur-containing amino acids. Annu RevBiochem 1983 52 187. 

Forman, H.J., Rotman, E.I. and Fisher, A.B. (1983). Roles of selenium and sulfur-containing amino acids in protection against oxygen toxicity. Lab. Invest. 49, 148-153. 

As a more sensitive detection method, MS can be very useful in amino acid determinations. For example, S-carboxymethyl-(R) cysteine or SCMC, is a mucolytic agent used in the treatment of respiratory diseases. The development of a method utilizing high performance IEC and atmospheric pressure ionization (API) mass spectrometry to quantify SCMC in plasma has been described.66 This method is simple (no derivatization needed), rapid (inn time 16 min.), sensitive (limit of quantification 200 ng/mL in human plasma), and has an overall throughput of more than 60 analyses per day. API-MS was used successfully with IEC to determine other sulfur-containing amino acids and their cyclic compounds in human urine.67 IEC has also been used as a cleanup step for amino acids prior to their derivatization and analysis by gas chromatography (GC), either alone or in conjunction with MS.68 69... 

Sulfur-containing amino acids, such as methionine and cystine, are probably the precursors of the mercaptans, sulfides, and disulfides.3 Dimethyl sulfide yields dimethyl sulfoxide and its oxidized product dimethyl... 

The second important issue related to commercial use of desulfurization biocatalysts is their inhibition by sulfate. The sulfur repression mechanism in most Rhodococcus species limits their use or activity in presence of sulfate- and sulfur-containing amino-acids such as cysteine, methionine, etc. To alleviate this problem, expression of the dsz genes under the control of alternate promoters has been investigated. 

PEC. The patent includes the production method for the biocatalyst, with a characteristic inhibitory effect on certain enzyme expression. The expression recombinant vector contains a promoter free from manifesting inhibition due to an inorganic sulfur compound or a sulfur-containing amino acid. The recombinant microorganism also contains a gene for desulfurizing the sulfur-containing heterocyclic compound. 

L.G. Shaidarova, S.A. Ziganshina, L.N. Tikhonova, and G.K. Budnikov, Electrocatalytic oxidation and flow-injection determination of sulfur-containing amino acids at graphite electrodes modified with a ruthenium hexacyanoferrate film. J. Anal. Chem. 58, 1144-1150 (2003). 

Sulfur-containing amino acids, especially L-methionine, serve as precursors for MT and the many materials derived from this compound, such as DMS, DMDS, DMTS, methyl thioacetate, etc. The most direct route for the L-methionine MT conversion is by demethiolation (Equation 4) catalyzed by methionine y-lyase, EC 4.4.1.11 ... 

As would be expected, the chemistry is complex. Unpleasant, off flavor odors usually derive from sulfur compounds, such as MT, DMS, DMDS, and DMTS, formed either enzymatically or non-enzymatically from sulfur-containing amino acids.35 Enzymatic routes to MT are essentially those previously considered (Section 11.1.2.4.5). Some DMS may derive by methylation of MT (Equation 8) with the donor, 5-adenosylmethionine, AdoMet ... 

In contrast to nucleic acids, which can be repaired after oxidative damage by excision and insertion mechanisms (see Chapter 28), the repair of oxidized proteins does not occur except the oxidized sulfur-containing amino acid residues [22]. Instead, oxidized proteins are... 

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