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  2. Oxidative deamination - Wikipedia

    en.wikipedia.org/wiki/Oxidative_deamination

    Glutamate can then be regenerated from α-KG via the action of transaminases or aminotransferase, which catalyze the transfer of an amino group from an amino acid to an α-keto acid. In this manner, an amino acid can transfer its amine group to glutamate, after which GDH can then liberate ammonia via oxidative deamination. This is a common ...

  3. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    The amino group is removed from the amino acid and converted to ammonia. The rest of the amino acid is made up of mostly carbon and hydrogen, and is recycled or oxidized for energy. Ammonia is toxic to the human system, and enzymes convert it to urea or uric acid by addition of carbon dioxide molecules (which is not considered a deamination ...

  4. N-terminus - Wikipedia

    en.wikipedia.org/wiki/N-terminus

    The amino end of an amino acid (on a charged tRNA) during the elongation stage of translation, attaches to the carboxyl end of the growing chain. Since the start codon of the genetic code codes for the amino acid methionine , most protein sequences start with a methionine (or, in bacteria, mitochondria and chloroplasts , the modified version N ...

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 (−NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation in the ribosome.

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    These amino acids are absorbed into the bloodstream to be transported to the liver and onward to the rest of the body. Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. [3] They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in ...

  7. Galactose oxidase - Wikipedia

    en.wikipedia.org/wiki/Galactose_oxidase

    Galactose oxidase contains 639 amino acids. [1] It is a single peptide monomer that has three β-structural domains. [1] [7] Domain 1 (residues 1-155) is a β-sandwich consisting of eight antiparallel β-strands. [3]

  8. Eukaryotic translation - Wikipedia

    en.wikipedia.org/wiki/Eukaryotic_translation

    During chain elongation, each additional amino acid is added to the nascent polypeptide chain in a three-step microcycle. The steps in this microcycle are (1) positioning the correct aminoacyl-tRNA in the A site of the ribosome, which is brought into that site by eEF1, (2) forming the peptide bond, and (3) shifting the mRNA by one codon ...

  9. L-amino-acid oxidase - Wikipedia

    en.wikipedia.org/wiki/L-amino-acid_oxidase

    The three substrates of the enzymatic reaction are an L-amino acid, water, and oxygen, whereas the three products are the corresponding α-keto acid (2-oxo acid), ammonia, and hydrogen peroxide. One example of the enzyme in action occurs with the conversion L-alanine into pyruvic acid (2-oxopropanoic acid), as shown in Figure 1.