Research Projects

Adenosine deaminase (ADA) is a crucial enzyme in the purine salvage pathway, catalyzing the irreversible deamination reaction from adenosine to inosine. Despite numerous investigations, there has been no published work on ADA MTB in recent years. The main aim is to understand the mechanistic role of ADA in the purine salvage pathway of Mycobacterium tuberculosis. A comprehensive understanding of the ADA MTB enzyme could lead to the development of a new drug discovery platform. ADA can interact with dipeptidyl peptidase 4 (DPP4), a serine protease that cleaves dipeptides from the N-terminus of polypeptides with proline at the penultimate position. This interaction has implications in signal transduction. In 1993, CD26 transfected Jurkat cell lines showed DPP4 present on T cells, which is considered in the CD26 cluster. ADA binds to DPP4 in bovine, rabbits, and humans, but the ADA-DPP4 complex does not form in rats and mice. In 2004, detailed information on molecular interactions between human ADA and human DPP4 was obtained, and preliminary research also found ADA MTB interacted with human DPP4. No one has explored ADA MTB interaction with human DPP4 or DPP4-like molecules present in bacteria.