AI Article Synopsis
- Leishmania braziliensis causes American Tegumentary Leishmaniasis (ATL), a significant tropical disease, and has two isoforms of the enzyme ENTPDase, which is linked to its infectivity.
- The study focused on the recombinant ENTPDase2 enzyme (rLbNTPDase2), showing it has apyrase activity, can break down various nucleotides, and needs divalent cations like calcium or magnesium for function.
- Characterization of rLbNTPDase2 revealed it works best at neutral to basic pH, is somewhat inhibited by certain compounds, and its low Km for ADP indicates it might be important for signaling processes, suggesting it could be a new
Article Abstract
Leishmania braziliensis is a pathogenic protozoan parasite that causes American Tegumentary Leishmaniasis (ATL), an important tropical neglected disease. ENTPDases are nucleotidases that hydrolyze intracellular and/or extracellular nucleotides. ENTPDases are known as regulators of purinergic signalling induced by extracellular nucleotides. Leishmania species have two isoforms of ENTPDase, and, particularly, ENTPDase2 seems to be involved in infectivity and virulence. In this study, we conducted the heterologous expression and biochemical characterization of the recombinant ENTPDase2 of L. braziliensis (rLbNTPDase2). Our results show that this enzyme is a canonical ENTPDase with apyrase activity, capable of hydrolysing triphosphate and diphosphate nucleotides, and it is dependent on divalent cations (calcium or magnesium). Substrate specificity was characterized as UDP>GDP>ADP>GTP>ATP=UTP. The enzyme showed optimal activity at a neutral to basic pH and was partially inhibited by suramin and DIDS. Furthermore, the low apparent Km for ADP suggests that the enzyme may play a role in adenosine-mediated signalling. The biochemical characterization of this enzyme can open new avenues for using LbNTPDase2 as a drug target.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11377403 | PMC |
| http://dx.doi.org/10.1007/s11302-023-09980-9 | DOI Listing |
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