Recombinant Human ADA2 beta protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

ADA2 beta also known as adenosine deaminase 2 beta performs catalytic deamination of adenosine to inosine a critical step in purine metabolism. The protein has a molecular mass of approximately 50 kDa. Expression of ADA2 beta primarily occurs in hematopoietic tissues such as the liver and spleen as well as in endothelial cells. The enzyme offers an important function in maintaining the balance of adenosine in the extracellular space.

Biological function summary

Adenosine deaminase activity from ADA2 beta impacts the modulation of immune responses and influences angiogenesis. The enzyme often operates as a part of a dimeric complex enhancing its stability and functional efficiency. It contributes to regulation of extracellular adenosine levels which in turn affects multiple signaling pathways involved in immune cell function and vascular biology.

Pathways

ADA2 beta serves an important role in the purine salvage pathway and the adenosine signaling pathway. The purine salvage pathway reuses purine bases for nucleotide synthesis where ADA2 beta helps convert excess adenosine ensuring efficient cellular metabolism. Adenosine accumulation is linked to immunosuppression positioning ADA2 beta as a regulatory agent. ADA2 beta shares functional interactions with proteins in the pathway like ADA and CD26 which have complementary roles in adenosine metabolism.

ADA2 beta links primarily to the genetic disease known as deficiency of adenosine deaminase 2 (DADA2) characterized by vascular and immune dysregulation. Mutations in ADA2 beta lead to systemic inflammation and vasculopathy. Additionally recent studies indicate a connection with certain types of vasculitis where the dysfunctional regulation of adenosine plays a role. ADA2 beta interacts with immune-related proteins such as TNF-alpha which can exacerbate inflammatory responses in these conditions.