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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

    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 ...

  5. 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.

  6. L-cystine - Wikipedia

    en.wikipedia.org/?title=L-cystine&redirect=no

    This page was last edited on 18 July 2006, at 19:25 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may ...

  7. Cystathionine gamma-lyase - Wikipedia

    en.wikipedia.org/wiki/Cystathionine_gamma-lyase

    The enzyme cystathionine γ-lyase (EC 4.4.1.1, CTH or CSE; also cystathionase; systematic name L-cystathionine cysteine-lyase (deaminating; 2-oxobutanoate-forming)) breaks down cystathionine into cysteine, 2-oxobutanoate (α-ketobutyrate), and ammonia: L-cystathionine + H 2 O = L-cysteine + 2-oxobutanoate + NH 3 (overall reaction)

  8. Cystinosis - Wikipedia

    en.wikipedia.org/wiki/Cystinosis

    Cystinosis is a lysosomal storage disease characterized by the abnormal accumulation of cystine, the oxidized dimer of the amino acid cysteine. [3] It is a genetic disorder that follows an autosomal recessive inheritance pattern.

  9. Cystine–lactose–electrolyte-deficient agar - Wikipedia

    en.wikipedia.org/wiki/Cystine–lactose...

    CLED agar (cystine–lactose–electrolyte-deficient agar or medium) is a valuable non-inhibitory growth medium used in the isolation and differentiation of urinary microbes. It contains cystine and lactose and is electrolyte -deficient; the latter trait prevents the swarming of Proteus species.