Adenosine deaminase 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.Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion.
ADA exists in both small form (as a monomer) and large form (as a dimer-complex). In the monomer form, the enzyme is a polypeptide chain, folded into eight strands of parallel ?/? barrels, which surround a central deep pocket that is the active site. In addition to the eight central ?-barrels and eight peripheral ?-helices, ADA also contains five additional helices: residues 19-76 fold into three helices, located between ?1 and ?1 folds; and two antiparallel carboxy-terminal helices are located across the amino-terminal of the ?-barrel.
Its primary function in humans is the development and maintenance of the immune system. However, the full physiological role of ADA is not yet completely understood.
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