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Oxydized Cysteine | Open Access Journals
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Environmental & Analytical Toxicology

ISSN: 2161-0525

Open Access

Oxydized Cysteine

Cysteine may be a semiessential proteinogenic aminoalkanoic acid with the formula HO2CCH(NH2)CH2SH. The thiol side chain in cysteine often participates in enzymatic reactions, as a nucleophile. The thiol is vulnerable to oxidation to offer the disulfide derivative cystine, which serves a crucial structural role in many proteins. When used as a artificial additive , it's the E number E920. it's encoded by the codons UGU and UGC. Cysteine has an equivalent structure as serine, but with one among its oxygen atoms replaced by sulfur; replacing it with selenium gives selenocysteine. Like other natural proteinogenic amino acids, cysteine has l chirality within the older d/l notation supported homology to d- and l-glyceraldehyde. within the newer R/S system of designating chirality, supported the atomic numbers of atoms near the asymmetric carbon, cysteine (and selenocysteine) have R chirality, due to the presence of sulfur (or selenium) as a second neighbour to the asymmetric carbon. The remaining chiral amino acids, having lighter atoms therein position, have S chirality. Like other common amino acids, cysteine (and its oxidized dimeric form cystine) is found in high-protein foods. Although classified as a nonessential aminoalkanoic acid , in rare cases, cysteine could also be essential for infants, the elderly, and individuals with certain metabolic diseases or that suffer from malabsorption syndromes. Cysteine can usually be synthesized by the physical body under normal physiological conditions if a sufficient quantity of methionine is out there .

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