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  2. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Cysteine ball and stick model spinning. 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.

  3. 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.

  4. Papain-like protease - Wikipedia

    en.wikipedia.org/wiki/Papain-like_protease

    In animals, especially in mammalian biology, members of the papain-like protease family are usually referred to as cysteine cathepsins—that is, the cysteine protease members of the group of proteases known as cathepsins (which includes cysteine, serine, and aspartic proteases).

  5. Cysteine metabolism - Wikipedia

    en.wikipedia.org/wiki/Cysteine_metabolism

    L-cysteine production pathways; Reactants → Enzyme Cofactors Notes O-acetyl-L-serine/hydrogen sulfide → cysteine synthase [9] pyridoxal phosphate not present in humans L-cystine/2 glutathione → glutathione-cystine transhydrogenase [10] cystathionine: → cystathionine γ-lyase [4] pyridoxal phosphate 3-mercapto-pyruvate: → cysteine ...

  6. Papain - Wikipedia

    en.wikipedia.org/wiki/Papain

    Papain-like cysteine proteinases are essentially synthesised as inactive proenzymes with N-terminal propeptide regions. The activation process of these enzymes includes the removal of propeptide regions, which serve a variety of functions in vivo and in vitro. The pro-region is required for the proper folding of the newly synthesised enzyme ...

  7. Cystathionine - Wikipedia

    en.wikipedia.org/wiki/Cystathionine

    Cystathionine is an intermediate in the synthesis of cysteine from homocysteine. It is produced by the transsulfuration pathway and is converted into cysteine by cystathionine gamma-lyase (CTH). Biosynthetically, cystathionine is generated from homocysteine and serine by cystathionine beta synthase (upper reaction in the diagram below).

  8. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    In this case NAS will act to disallow the binding of CysB to its own DNA sequence. OAS is a precursor of NAS, cysteine itself can inhibit CysE which functions to create OAS. Without the necessary OAS, NAS will not be produced and cysteine will not be produced. There are two other negative regulators of cysteine.

  9. Biochemistry - Wikipedia

    en.wikipedia.org/wiki/Biochemistry

    Molecular biology is the study of molecular underpinnings of the biological phenomena, focusing on molecular synthesis, modification, mechanisms and interactions. The central dogma of molecular biology , where genetic material is transcribed into RNA and then translated into protein , despite being oversimplified, still provides a good starting ...