enow.com Web Search

Search results

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

    en.wikipedia.org/wiki/Deamination

    Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy.

  3. Phenylalanine ammonia-lyase - Wikipedia

    en.wikipedia.org/wiki/Phenylalanine_ammonia-lyase

    [9] [10] The reaction catalyzed by PAL is a spontaneous elimination reaction rather than an oxidative deamination. [11] The cofactor 3,5-dihydro-5-methyldiene-4H-imidazol-4-one (MIO) is involved in the reaction and sits atop the positive pole of three polar helices in the active site, which helps to increase its electrophilicity. [12]

  4. Oxidative deamination - Wikipedia

    en.wikipedia.org/wiki/Oxidative_deamination

    Oxidative deamination is a form of deamination that generates α-keto acids and other oxidized products from amine-containing compounds, and occurs primarily in the liver. [1] Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid ...

  5. Protein catabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_catabolism

    Oxidative deamination is the first step to breaking down the amino acids so that they can be converted to sugars. The process begins by removing the amino group of the amino acids. The amino group becomes ammonium as it is lost and later undergoes the urea cycle to become urea, in the liver. It is then released into the blood stream, where it ...

  6. Deamidation - Wikipedia

    en.wikipedia.org/wiki/Deamidation

    Deamidation reaction of Asn-Gly (top right) to Asp-Gly (at left) or iso(Asp)-Gly (in green at bottom right) Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group.

  7. Keto acid - Wikipedia

    en.wikipedia.org/wiki/Keto_acid

    They often arise by oxidative deamination of amino acids, and reciprocally, they are precursors to the same. Alpha-keto acids possesses extensive chemistry as acylation agents. [3] Furthermore, alpha-keto acids such as phenylpyruvic acid are endogenous sources for carbon monoxide (as a gasotransmitter) and pharmaceutical prodrug scaffold. [4]

  8. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    Transamination is a chemical reaction that transfers an amino group to a ketoacid to form new amino acids.This pathway is responsible for the deamination of most amino acids. This is one of the major degradation pathways which convert essential amino acids to non-essential amino acids (amino acids that can be synthesized de novo by the organism).

  9. Diphenylamine - Wikipedia

    en.wikipedia.org/wiki/Diphenylamine

    Diphenylamine is manufactured by the thermal deamination of aniline over oxide catalysts: 2 C 6 H 5 NH 2 → (C 6 H 5) 2 NH + NH 3. It is a weak base, with a K b of 10 −14. With strong acids, it forms salts. For example, treatment with sulfuric acid gives the bisulfate [(C 6 H 5) 2 NH 2] + [HSO 4] − as a white or yellowish powder with m.p ...