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  2. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    Only the L-stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. [5] Its name is derived from the Latin for silk, sericum. Serine's structure ...

  3. Phosphatidylserine - Wikipedia

    en.wikipedia.org/wiki/Phosphatidylserine

    Phosphatidylserine (abbreviated Ptd-L-Ser or PS) is a phospholipid and is a component of the cell membrane. [1] It plays a key role in cell cycle signaling, specifically in relation to apoptosis . It is a key pathway for viruses to enter cells via apoptotic mimicry . [ 2 ]

  4. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Used in proteins and as a storage for ammonia, it is the most abundant amino acid in the body. Arginine: R Arg Functionally similar to lysine. Serine: S Ser Serine and threonine have a short group ended with a hydroxyl group. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes.

  5. Sphingomyelin - Wikipedia

    en.wikipedia.org/wiki/Sphingomyelin

    The synthesis of sphingomyelin involves the enzymatic transfer of a phosphocholine from phosphatidylcholine to a ceramide. The first committed step of sphingomyelin synthesis involves the condensation of L-serine and palmitoyl-CoA. This reaction is catalyzed by serine palmitoyltransferase. The product of this reaction is reduced, yielding ...

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    The steps of protein synthesis include transcription, translation, and post translational modifications. During transcription, RNA polymerase transcribes a coding region of the DNA in a cell producing a sequence of RNA, specifically messenger RNA (mRNA). This mRNA sequence contains codons: 3 nucleotide long segments that code for a specific ...

  7. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    This enzyme is the key regulatory step in this pathway. Phosphoglycerate dehydrogenase is regulated by the concentration of serine in the cell. At high concentrations this enzyme will be inactive and serine will not be produced. At low concentrations of serine the enzyme will be fully active and serine will be produced by the bacterium. [13]

  8. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    Serine protease, as released by mast cells, is an important diagnostic marker for type 1 hypersensitivity reactions e.g., anaphylaxis. More useful than histamine due to the longer half-life , meaning it remains in the system for a clinically useful length of time.

  9. Serine hydroxymethyltransferase - Wikipedia

    en.wikipedia.org/wiki/Serine_hydroxymethyl...

    PyMol rendered crystal structure of serine hydroxymethyltransferase. Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate (PLP) (Vitamin B 6) dependent enzyme (EC 2.1.2.1) which plays an important role in cellular one-carbon pathways by catalyzing the reversible, simultaneous conversions of L-serine to glycine and tetrahydrofolate (THF) to 5,10-methylenetetrahydrofolate (5,10-CH 2 ...