Adenosine deaminase Streptococcus thermophilus, recombinant

Adenosine deaminase is a single polypeptide chain having eight parallel strands of α⁄β barrels. The molecular weight is found to be approximately 38,000 Da. The deep pocket at the COOH-terminal of the β barrel, which contains zinc as the co-factor, serves as the active site. It is ubiquitously found in wide variety of microorganisms, plants, and invertebrates.

Adenosine deaminase was used to study its inhibitory effect on cerebrocortical vasodilatation (brain activation) and hypoxia. It was also used for the comparison of the inhibition by two adenosine analogs, N6-phenylisopropyladenosine and 5′-N-ethylcarboxamideadenosine of glycerol production by adipocytes

Adenosine deaminase is an active enzyme in purine metabolism, which mainly catalyzes the irreversible hydrolytic deamination of adenosine and deoxyadenosine to inosine and deoxyinosine, respectively. It is adequately present in mammalian tissue, and its deficiency leads to combined immunodeficiency disease. It is also present in all mammalian cells that play a key role in differentiation and maturation of lymphoid system.

One unit will deaminate 1.0 μmole of adenosine to inosine per min at pH 7.5 at 25°C.