enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Threonine - Wikipedia

    en.wikipedia.org/wiki/Threonine

    Threonine (symbol Thr or T) [2] is an amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), a carboxyl group (which is in the deprotonated −COO − form when dissolved in water), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid.

  3. Threonine protease - Wikipedia

    en.wikipedia.org/wiki/Threonine_protease

    Threonine protease. Threonine proteases are a family of proteolytic enzymes harbouring a threonine (Thr) residue within the active site. The prototype members of this class of enzymes are the catalytic subunits of the proteasome, however, the acyltransferases convergently evolved the same active site geometry and mechanism.

  4. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates.

  5. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially protonated), classifying it as a ...

  6. Threonine ammonia-lyase - Wikipedia

    en.wikipedia.org/wiki/Threonine_ammonia-lyase

    Threonine ammonia-lyase (EC 4.3.1.19, systematic name L-threonine ammonia-lyase (2-oxobutanoate-forming), also commonly referred to as threonine deaminase or threonine dehydratase, is an enzyme responsible for catalyzing the conversion of L -threonine into α-ketobutyrate and ammonia: L -threonine = 2-oxobutanoate + NH 3 (overall reaction)

  7. 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.

  8. Protonation - Wikipedia

    en.wikipedia.org/wiki/Protonation

    Protonation. In chemistry, protonation (or hydronation) is the adding of a proton (or hydron, or hydrogen cation), usually denoted by H +, to an atom, molecule, or ion, forming a conjugate acid. [1] (. The complementary process, when a proton is removed from a Brønsted–Lowry acid, is deprotonation.) Some examples include. The protonation of ...

  9. Cellular respiration - Wikipedia

    en.wikipedia.org/wiki/Cellular_respiration

    Cellular respiration is the process by which biological fuels are oxidised in the presence of an inorganic electron acceptor, such as oxygen, to produce large amounts of energy and drive the bulk production of ATP. Anaerobic respiration is used by microorganisms, either bacteria or archaea, in which neither oxygen (aerobic respiration) nor ...