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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 ...
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).
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Adenosine deaminase (also known as adenosine aminohydrolase, or ADA) is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues.
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 .
Other names in common use include D-hydroxyaminoacid dehydratase, D-serine dehydrase, D-hydroxy amino acid dehydratase, D-serine hydrolase, D-serine dehydratase (deaminating), D-serine deaminase, and D-serine hydro-lyase (deaminating).
Guanine deaminase also known as cypin, guanase, guanine aminase, GAH, and guanine aminohydrolase is an aminohydrolase enzyme which converts guanine to xanthine. [ 5 ] [ 6 ] [ 7 ] Cypin is a major cytosolic protein that interacts with PSD-95 .