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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. Its primary function in humans is the development and maintenance of the immune system. [5]
The enzyme adenosine deaminase is encoded by the ADA gene on chromosome 20. [1] ADA deficiency is inherited in an autosomal recessive manner. This means the defective gene responsible for the disorder is located on an autosome (chromosome 20 is an autosome), and two copies of the defective gene (one inherited from each parent) are required in order to be born with the disorder.
Without myoadenylate deaminase, heavy activity causes adenosine to be released into the cell or perfused into the surrounding tissues. Fatigue and sedation after heavy exertion can be caused by excess adenosine in the cells which signals muscle fiber to feel fatigued. In the brain, excess adenosine decreases alertness and causes sleepiness.
Eloise "Elo" R. Giblett (January 17, 1921 – September 16, 2009) was an American genetic scientist and hematologist who discovered the first recognized immunodeficiency disease, adenosine deaminase deficiency. [1]
The protein product of this gene, adenosine deaminase 2 (ADA2), is an extracellular enzyme that breaks down adenosine and may also serve as a growth factor. Pathogenic mutations decrease this enzymatic activity in patient blood, leading to disease manifestations. However, mutational status and residual enzyme activity levels do not explicitly ...
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
When the enzyme adenosine deaminase is deficient in the body, the result is a toxic build-up of metabolites that impair lymphocyte development and function. [9] Many ADA deficient children with SCID have been treated with the polyethylene glycol-conjugated adenosine deaminase (PEG-ADA) enzyme.
Patients with adenosine deaminase deficiency (ADA) tend to have elevated intracellular dATP concentrations because adenosine deaminase normally curbs adenosine levels by converting it into inosine. [3] [4] Deficiency of this deaminase also causes immunodeficiency. [5]