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  2. Sulfur assimilation - Wikipedia

    en.wikipedia.org/wiki/Sulfur_assimilation

    The synthesis of O-acetylserine is catalyzed by serine acetyltransferase and together with O-acetylserine (thiol)lyase it is associated as enzyme complex named cysteine synthase. The formation of cysteine is the direct coupling step between sulfur (sulfur metabolism) and nitrogen assimilation in plants.

  3. Cell-free protein synthesis - Wikipedia

    en.wikipedia.org/wiki/Cell-free_protein_synthesis

    Cell-free protein synthesis, also known as in vitro protein synthesis or CFPS, is the production of protein using biological machinery in a cell-free system, that is, without the use of living cells. The in vitro protein synthesis environment is not constrained by a cell wall or homeostasis conditions necessary to maintain cell viability. [ 1 ]

  4. 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.

  5. Homocysteine - Wikipedia

    en.wikipedia.org/wiki/Homocysteine

    It is a homologue of the amino acid cysteine, differing by an additional methylene bridge (-CH 2-). It is biosynthesized from methionine by the removal of its terminal C ε methyl group. In the body, homocysteine can be recycled into methionine or converted into cysteine with the aid of vitamin B 6, B 9, and B 12. [3]

  6. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein.

  7. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    The synthesis of aspartate kinase (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by lysine, isoleucine, and threonine, which prevents the synthesis of the amino acids derived from aspartate. So, in addition to inhibiting the first enzyme of the aspartate ...

  8. 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.

  9. Metalloproteinase - Wikipedia

    en.wikipedia.org/wiki/Metalloproteinase

    The serine, threonine and cysteine peptidases utilise the amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated water molecule.

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