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  2. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    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 was established in 1902. [6] [7]

  3. Serine (data page) - Wikipedia

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

    Systematic name:-2-amino-3-hydroxypropanoic acid Abbreviations: S, Ser Synonyms: ... ^a EINECS for Serine ^a CID 617 from PubChem ^a CID 5951 from PubChem

  4. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all superfamilies of serine protease enzymes. The triad is a coordinated structure consisting of three amino acids: His 57, Ser 195 (hence the name "serine protease") and Asp 102. These three key amino acids each play an essential role in the ...

  5. Phosphatidylserine - Wikipedia

    en.wikipedia.org/wiki/Phosphatidylserine

    Phosphatidylserine (PS) is the major acidic phospholipid class that accounts for 13–15% of the phospholipids in the human cerebral cortex. [7] In the plasma membrane, PS is localized exclusively in the cytoplasmic leaflet where it forms part of protein docking sites necessary for the activation of several key signaling pathways.

  6. Essential amino acid - Wikipedia

    en.wikipedia.org/wiki/Essential_amino_acid

    These six are alanine, aspartic acid, asparagine, glutamic acid, serine, [2] and selenocysteine (considered the 21st amino acid). Pyrrolysine (considered the 22nd amino acid), [3] which is proteinogenic only in certain microorganisms, is not used by and therefore non-essential for most organisms, including humans.

  7. Serine/threonine-specific protein kinase - Wikipedia

    en.wikipedia.org/wiki/Serine/threonine-specific...

    Many serine/threonine protein kinases do not have their own individual EC numbers and use 2.7.11.1, "non-specific serine/threonine protein kinase". This entry is for any enzyme that phosphorylates proteins while converting ATP to ADP (i.e., ATP:protein phosphotransferases.) [10] 2.7.11.37 "protein kinase" was the former generic placeholder and was split into several entries (including 2.7.11.1 ...

  8. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Common in collagen, it often undergoes a post-translational modification to hydroxyproline. Glutamine: Q Gln Similar to glutamic acid, Gln contains an amide group where Glu has a carboxyl. 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

  9. SERTM2 - Wikipedia

    en.wikipedia.org/wiki/SERTM2

    SERTM2, also known as the Serine Rich And Transmembrane Domain Containing 2, is a protein which in humans is encoded by the SERTM2 gene. The SERTM2 protein is a transmembrane protein located in the intracellular membrane and active in membrane-bound organelles .