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  2. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in the industrial synthesis of L-cysteine for example.

  3. Schöllkopf method - Wikipedia

    en.wikipedia.org/wiki/Schöllkopf_method

    The Schöllkopf method or Schöllkopf Bis-Lactim Amino Acid Synthesis is a method in organic chemistry for the asymmetric synthesis of chiral amino acids. [1] [2] The method was established in 1981 by Ulrich Schöllkopf. [3] [4] [5] In it glycine is a substrate, valine a chiral auxiliary and the reaction taking place an alkylation.

  4. Strecker amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Strecker_amino_acid_synthesis

    The Strecker amino acid synthesis, also known simply as the Strecker synthesis, is a method for the synthesis of amino acids by the reaction of an aldehyde with cyanide in the presence of ammonia. The condensation reaction yields an α-aminonitrile, which is subsequently hydrolyzed to give the desired amino acid.

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino acids are known as non-essential amino acids. Essential amino acids require intermediates not present in the human body. These intermediates must be ingested, mostly from eating other organisms. [6]

  6. Cyanosulfidic prebiotic synthesis - Wikipedia

    en.wikipedia.org/wiki/Cyanosulfidic_Prebiotic...

    Cyanosulfidic prebiotic synthesis is a proposed mechanism for the origin of the key chemical building blocks of life. [1] It involves a systems chemistry approach to synthesize the precursors of amino acids, ribonucleotides, and lipids using the same starting reagents and largely the same plausible early Earth conditions. [2]

  7. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    The different amino acids are identified by the functional group. As a result of the three different groups attached to the α-carbon, amino acids are asymmetrical molecules. For all standard amino acids, except glycine, the α-carbon is a chiral center. In the case of glycine, the α-carbon has two hydrogen atoms, thus adding symmetry to this ...

  8. Stable isotope composition of amino acids - Wikipedia

    en.wikipedia.org/wiki/Stable_isotope_composition...

    The abundance of 15 N in some amino acids reflects an organism's position in a food web. This is due to the ways organisms metabolize different amino acids when they are consumed. Trophic amino acids (TrAAs) are first deaminated, meaning that the amino group is removed to produce an alpha-keto acid carbon skeleton.

  9. Click chemistry - Wikipedia

    en.wikipedia.org/wiki/Click_chemistry

    The synthesis of luciferin exemplifies another strategy of isolating reaction partners, which is to take advantage of rarely-occurring, natural groups such as the 1,2-aminothiol, which appears only when a cysteine is the final N' amino acid in a protein. Their natural selectivity and relative bioorthogonality is thus valuable in developing ...