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  2. Cysteine - Wikipedia

    en.wikipedia.org/wiki/Cysteine

    Cysteine is chiral, but both D and L-cysteine are found in nature. L‑Cysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. [8] Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Greek κύστις kýstis, "bladder". [9]

  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. Cysteine metabolism - Wikipedia

    en.wikipedia.org/wiki/Cysteine_metabolism

    Cysteine metabolism refers to the biological pathways that consume or create cysteine. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems. The pathways of different amino acids and other metabolites interweave and overlap to creating complex systems.

  5. Cysteine (data page) - Wikipedia

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

    The complete data for Cysteine. General information. Chemical formula: C 3 H 7 N O 2 S ...

  6. Papain-like protease - Wikipedia

    en.wikipedia.org/wiki/Papain-like_protease

    The negatively charged cysteine thiolate functions as a nucleophile. [1] [2] Additional neighboring residues—aspartate, asparagine, or glutamine—position the catalytic residues; [1] [2] in papain, the required catalytic residues cysteine, histidine, and aspartate are sometimes called the catalytic triad (similar to serine proteases). [11]

  7. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    Unlike cysteine and serine, threonine is a secondary hydroxyl (i.e. has a methyl group). This methyl group greatly restricts the possible orientations of triad and substrate as the methyl clashes with either the enzyme backbone or histidine base. [ 2 ]

  8. Cystine/glutamate transporter - Wikipedia

    en.wikipedia.org/wiki/Cystine/glutamate_transporter

    Cystine is a dimer consisting of two cysteine molecules and the formation of a disulfide bond. This amino acid is a rate limiting substrate used in the SLC7A11 cystine/glutamate transporter and is usually imported into the cell. Cysteine-158 is specifically used in the formation of the disulfide bridge for the protein structure of system Xc-. [9]

  9. Cystinuria - Wikipedia

    en.wikipedia.org/wiki/Cystinuria

    Cystinuria is a cause of recurrent kidney stones. It is a disease involving the defective transepithelial transport of cystine and dibasic amino acids in the kidney and intestine, and is one of many causes of kidney stones.