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  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.

  3. Amidase - Wikipedia

    en.wikipedia.org/wiki/Amidase

    Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways : urea cycle and metabolism of amino groups , phenylalanine metabolism , tryptophan metabolism , cyanoamino acid metabolism , benzoate degradation via coa ligation ...

  4. Diagnostic microbiology - Wikipedia

    en.wikipedia.org/wiki/Diagnostic_Microbiology

    The phenylalanine deaminase test is used to tell whether an organism can produce the enzyme deaminase. Deaminase is the enzyme that can deaminate the amino acid phenylalanine into the products ammonia and phenylpyruvic acid. The test is performed by adding phenylalanine to the growth medium and allowing growth to occur.

  5. 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)

  6. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Download QR code; Print/export Download as PDF; Printable version; In other projects ... Adenosine deaminase (EC 3.5.4.4) GTP cyclohydrolase I ...

  7. Oxidative deamination - Wikipedia

    en.wikipedia.org/wiki/Oxidative_deamination

    Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid oxidase and L-amino acid oxidase is present only in the liver and kidney. [2]

  8. Porphobilinogen deaminase - Wikipedia

    en.wikipedia.org/wiki/Porphobilinogen_deaminase

    The most well-known health issue involving porphobilinogen deaminase is acute intermittent porphyria, an autosomal dominant genetic disorder where insufficient hydroxymethylbilane is produced, leading to a build-up of porphobilinogen in the cytoplasm. This is caused by a gene mutation that, in 90% of cases, causes decreased amounts of enzyme.

  9. ATP deaminase - Wikipedia

    en.wikipedia.org/wiki/ATP_deaminase

    In enzymology, an ATP deaminase (EC 3.5.4.18) is an enzyme that catalyzes the chemical reaction ATP + H 2 O ⇌ {\displaystyle \rightleftharpoons } ITP + NH 3 Thus, the two substrates of this enzyme are ATP and H 2 O , whereas its two products are ITP and NH 3 .