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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.
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 ...
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)
Full PBG Deaminase Mechanism. The first step is believed to involve an E1 elimination of ammonia from porphobilinogen, generating a carbocation intermediate (1). [10] This intermediate is then attacked by the dipyrrole cofactor of porphobilinogen deaminase, which after losing a proton yields a trimer covalently bound to the enzyme (2).
Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene. [5] [6] [7] This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several ...
A nucleotidase creates adenosine, then adenosine deaminase creates inosine; Alternatively, AMP deaminase creates inosinic acid, then a nucleotidase creates inosine; Purine nucleoside phosphorylase acts upon inosine to create hypoxanthine; Xanthine oxidase catalyzes the biotransformation of hypoxanthine to xanthine
In enzymology, an arginine deiminase (EC 3.5.3.6) is an enzyme that catalyzes the chemical reaction. L-arginine + H 2 O L-citrulline + NH 3. Thus, the two substrates of this enzyme are L-arginine and H 2 O, whereas its two products are L-citrulline and NH 3.
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.