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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.
3,4-dihydroxyphenylalanine oxidative deaminase (EC 1.13.12.15, 3,4-dihydroxy-L-phenylalanine: oxidative deaminase, oxidative deaminase, DOPA oxidative deaminase, DOPAODA) is an enzyme with systematic name 3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating). [1] This enzyme catalyses the following chemical reaction
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).
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.
Adenosine-phosphate deaminase is found in most, if not all organisms in all tissues, however, muscle tissue is the richest source. [6] The basic pathway of adenosine-phosphate deaminase is to replace a C-N bond of a 5'-AMP to replace the carboxyl group forming 5'-IMP. 5'-IMP is then catalyzed by Inosine-5'-monophosphate dehydrogenase (IMPDH) in guanine nucleotide biosynthesis.
Adenosine monophosphate deaminase deficiency type 1 or AMPD1, is a human metabolic disorder in which the body consistently lacks the enzyme AMP deaminase, [1] in sufficient quantities. This may result in exercise intolerance, muscle pain and muscle cramping. The disease was formerly known as myoadenylate deaminase deficiency (MADD).
Phenylalanine ammonia lyase is specific for L-phenylalanine, and to a lesser extent, L-tyrosine. [9] [10] The reaction catalyzed by PAL is a spontaneous elimination reaction rather than an oxidative deamination.