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  2. Akabori amino-acid reaction - Wikipedia

    en.wikipedia.org/wiki/Akabori_amino-acid_reaction

    There are several Akabori amino acid reactions, which are named after Shirō Akabori (Japanese: 赤堀 四郎) (1900–1992), a Japanese chemist. In the first reaction, an α- amino acid is oxidised and undergoes decarboxylation to give an aldehyde at the former α position by heating with oxygen in the presence of a reducing sugar .

  3. Decarboxylation - Wikipedia

    en.wikipedia.org/wiki/Decarboxylation

    In the related Hammick reaction, uncatalyzed decarboxylation of a picolinic acid gives a stable carbene that attacks a carbonyl electrophile. Oxidative decarboxylations are generally radical reactions. These include the Kolbe electrolysis and Hunsdiecker-Kochi reactions. The Barton decarboxylation is an unusual radical reductive decarboxylation.

  4. Arginine decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Arginine_decarboxylase

    The process consumes a proton in the decarboxylation and employs a pyridoxal-5'-phosphate (PLP) cofactor, similar to other enzymes involved in amino acid metabolism, such as ornithine decarboxylase and glutamine decarboxylase. [1] It is found in bacteria and virus, though most research has so far focused on forms of the enzyme in bacteria.

  5. Ornithine decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Ornithine_decarboxylase

    The enzyme ornithine decarboxylase (EC 4.1.1.17, ODC) catalyzes the decarboxylation of ornithine (a product of the urea cycle) to form putrescine. This reaction is the committed step in polyamine synthesis. [1] In humans, this protein has 461 amino acids and forms a homodimer. [2] In humans, ornithine decarboxylase (ODC) is expressed by the ...

  6. Diaminopimelate decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Diaminopimelate_decarboxylase

    This enzyme is generally dimeric with each monomer containing two domains. [5] The first domain is the N-terminal α/β-barrel that binds the PLP to the active site lysine residue. [3] [4] [5] The second domain is the C-terminal β-sandwich. [4] [5] The active site is formed from residues present in both domains resulting in two active sites ...

  7. Ketonic decarboxylation - Wikipedia

    en.wikipedia.org/wiki/Ketonic_decarboxylation

    Ketonic decarboxylation (also known as decarboxylative ketonization) is a type of organic reaction and a decarboxylation converting two equivalents of a carboxylic acid (R−C(=O)OH) to a symmetric ketone (R 2 C=O) by the application of heat. It can be thought of as a decarboxylative Claisen condensation of two identical molecules.

  8. Malonyl-CoA decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Malonyl-CoA_decarboxylase

    Malonyl-CoA decarboxylase is firstly processed as a pro-protein or proenzyme, in which the transit peptide, whose role is to transport the enzyme to a specific organelle (in this case the mitochondria), comprises the first 39 amino acids (beginning with a methionine and ending with an alanine). The polypeptide chain in the mature protein is ...

  9. Acetoacetate decarboxylase - Wikipedia

    en.wikipedia.org/wiki/Acetoacetate_decarboxylase

    The reaction of acetoacetate decarboxylase with p-chloromercuriphenylsulfonate (CMS) results in decreased catalytic activity upon two equivalents of CMS per enzyme subunit. [15] CMS interacts with two sulfhydryl groups located on each enzyme subunit. Further inactivation occurs upon addition of a third equivalent of CMS per subunit.