Unlocking the Potential of ATP6V1E2: A Drug Target and Biomarker for Proton-Translocating ATPase Subunits

Target Name: ATP6V1E2

NCBI ID: G90423

ATP6V1E2

Unlocking the Potential of ATP6V1E2: A Drug Target and Biomarker for Proton-Translocating ATPase Subunits

ATP (adenosine triphosphate) is the primary energy source for all cell types, and its production and breakdown are tightly regulated processes. One of the key enzymes involved in ATP production is the proton-translocating ATPase subunit E1 (ATP6V1E2), which is a key subunit of the ATP-dependent proton motive force (PMF) complex. In this article, we will explore the biology and potential drug targets of ATP6V1E2.

The Proton-Translocating ATPase Subunit E1

ATP6V1E2 is a 22kDa protein that is expressed in most eukaryotic cells. It is a key subunit of the PMF complex, which is responsible for generating the energy by protonation of the ADP molecule. The PMF is a protein-protein interaction (PPI) complex that consists of multiple subunits, including ATP6V1E2, ATP6V2E2, and ATP6V0E2. ATP6V1E2 is the catalytic subunit of the PMF and is responsible for the protonation of ADP.

ATP6V1E2 is a proton-translocating ATPase, which means that it uses protonation as a means of generating ATP energy. The ATP molecule is a high-energy molecule that is derived from ADP through the transfer of a phosphate group. Protonation of the ADP molecule to ATP involves the transfer of a proton from the PMF to the ADP molecule. This process requires the use of ATP6V1E2, which catalyzes the reaction by transferring a proton from ATP to ADP.

The ATP6V1E2-Catalyzed Proton Transfer

The ATP6V1E2-catalyzed proton transfer reaction is a critical step in the ATP production process. The reaction involves the transfer of a proton from ATP to ADP, which generates ATP. The ATP6V1E2 enzyme uses a unique substrate specificity to catalyze this reaction. It can only catalyze the transfer of a proton from ATP to ADP, and not from ADP to ATP.

The ATP6V1E2-catalyzed proton transfer reaction is a critical step in the ATP production process. The transfer of a proton from ATP to ADP generates ATP, which is the energy source for the cell. The ATP6V1E2 enzyme uses a unique substrate specificity to catalyze this reaction.

Drug Targets and Biomarkers

Drugs that target the ATP6V1E2 enzyme have the potential to be effective in treating a variety of conditions. One of the main targets of these drugs is the treatment of bacterial infections, such as salmonella and staphylococcus. These bacteria use ATP to maintain their growth and survival, and the inhibition of ATP6V1E2 could be a valuable therapeutic approach.

In addition to its potential in treating bacterial infections, the ATP6V1E2 enzyme is also a potential biomarker for various diseases. The expression of ATP6V1E2 has been observed in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. The inhibition of ATP6V1E2 has been shown to be effective in treating these diseases, suggesting that it may be a valuable biomarker and drug target.

Conclusion

In conclusion, the proton-translocating ATPase subunit E1 (ATP6V1E2) is a key enzyme involved in ATP production and has the potential to be a drug target and biomarker. The inhibition of ATP6V1E2 has been shown to be effective in treating bacterial infections and various diseases, suggesting that it may be a valuable therapeutic approach in the future. Further research is needed to fully understand the biology and potential drug targets of ATP6V1E2.

Protein Name: ATPase H+ Transporting V1 Subunit E2

Functions: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment

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