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  2. Cystine - Wikipedia

    en.wikipedia.org/wiki/Cystine

    Cystine is the oxidized derivative of the amino acid cysteine and has the formula (SCH 2 CH(NH 2)CO 2 H) 2.It is a white solid that is poorly soluble in water. As a residue in proteins, cystine serves two functions: a site of redox reactions and a mechanical linkage that allows proteins to retain their three-dimensional structure.

  3. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Cysteine (/ ˈ s ɪ s t ɪ iː n /; [5] symbol Cys or C [6]) is a semiessential [7] proteinogenic amino acid with the formula HOOC−CH(−NH 2)−CH 2 −SH. The thiol side chain in cysteine enables the formation of disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine ...

  4. Cysteine (data page) - Wikipedia

    en.wikipedia.org/wiki/Cysteine_(data_page)

    Download as PDF; Printable version; In other projects ... The complete data for Cysteine. General information. Chemical formula: C 3 H ... Structure. Crystal data ...

  5. Papain-like protease - Wikipedia

    en.wikipedia.org/wiki/Papain-like_protease

    Papain-like proteases share a common catalytic dyad active site featuring a cysteine amino acid residue that acts as a nucleophile. [1] The human genome encodes eleven cysteine cathepsins which have a broad range of physiological functions. [3] In some parasites papain-like proteases have roles in host invasion, such as cruzipain from ...

  6. Aminopeptidase - Wikipedia

    en.wikipedia.org/wiki/Aminopeptidase

    Cysteine aminopeptidases, on the other hand, rely on a cysteine amino acid to perform catalysis. These enzymes are part of a broader group of cysteine proteases , all of which carve up proteins by using a nucleophilic cysteine thiol along with one or two other catalytic amino acids in a diad or triad.

  7. γ-L-Glutamyl-L-cysteine - Wikipedia

    en.wikipedia.org/wiki/Γ-L-Glutamyl-L-cysteine

    γ-L-Glutamyl-L-cysteine, also known as γ-glutamylcysteine (GGC), is a dipeptide found in animals, plants, fungi, some bacteria, and archaea. It has a relatively unusual γ-bond between the constituent amino acids , L -glutamic acid and L -cysteine and is a key intermediate in the γ-glutamyl cycle first described by Meister in the 1970s.

  8. Cysteine—tRNA ligase - Wikipedia

    en.wikipedia.org/wiki/Cysteine—tRNA_ligase

    In enzymology, a cysteine—tRNA ligase (EC 6.1.1.16) is an enzyme that catalyzes the chemical reaction. ATP + L-cysteine + tRNACys AMP + diphosphate + L-cysteinyl-tRNACys. The 3 substrates of this enzyme are ATP, L-cysteine, and tRNA(Cys), whereas its 3 products are AMP, diphosphate, and L-cysteinyl-tRNA(Cys).

  9. S-Methylcysteine - Wikipedia

    en.wikipedia.org/wiki/S-Methylcysteine

    S-Methylcysteine is not genetically coded, but it arises by post-translational methylation of cysteine. One pathway involves methyl transfer from alkylated DNA by zinc-cysteinate-containing repair enzymes. [2] [3] S-Methylcysteine sulfoxide is an oxidized derivative of S-methylcysteine that is found in onions. [4]