ATP5F1EP2: A Potential Drug Target for Mitochondrial Disorders

Target Name: ATP5F1EP2

NCBI ID: G432369

ATP5F1EP2

Other Name(s): ATP synthase, H+ transporting, mitochondrial F1 complex, epsilon subunit pseudogene 2 | ATP5EP2 | ATP synthase F1 subunit epsilon pseudogene 2

ATP5F1EP2: A Potential Drug Target for Mitochondrial Disorders

Introduction

ATP (adenosine triphosphate) is an essential energy carrier molecule that plays a pivotal role in various cellular processes, including muscle contraction, nerve transmission, and chromatin remodeling. The synthase ATP synthase (ATP synthase) is the rate limiting step in the ATP biosynthesis pathway, and it functions as a protein that catalyzes the transfer of a phosphate group from an inorganic phosphate to the ADP molecule to produce ATP. The H+ transporting ATP synthase (H+ ATP synthase) is a subunit of the ATP synthase that is responsible for transporting H+ ions from the cytoplasm to the mitochondrial matrix and is a known drug target for various diseases, including heart failure, hypertension, and cancer.

The mitochondrial F1 complex is a protein complex that is composed of several subunits, including the alpha, beta, gamma, delta, and epsilon subunits, that work together to produce ATP from ADP and Pi in the cytoplasm. The epsilon subunit pseudogene 2 (ATP5F1EP2 ) is one of the subunits of the F1 complex that is involved in the production of ATP from Pi.

Properties of ATP5F1EP2

ATP5F1EP2 is a 26 kDa protein that consists of 154 amino acid residues. It has a molecular weight of 43,811 Da and a calculated pI of 6.3. ATP5F1EP2 is predominantly monomeric and has a localization in the cytoplasm. It can form a stable complex with the alpha subunit of H+ ATP synthase and the alpha subunit of the F1 complex.

Function of ATP5F1EP2

ATP5F1EP2 is a key subunit of the F1 complex that is involved in the production of ATP from Pi. It functions as a catalytic subunit for the alpha subunit of H+ ATP synthase and is responsible for the transfer of a phosphate group from Pi to the alpha subunit of H+ ATP synthase. The transfer of the phosphate group from Pi to the alpha subunit of H+ ATP synthase is the rate-limiting step in the production of ATP and is critical for the function of the H+ ATP synthase.

Mutations in the ATP5F1EP2 gene have been linked to various mitochondrial disorders, including mutations in the ATP synthase gene that are associated with vesicle transport disorders, such as MELAS (Mitochondrial Encephalomyopathy, Lactic Acidosis, and Stroke-like episodes), and mutations in the H+ ATP synthase gene that are associated with a defect in ATP production and the development of certain neurodegenerative diseases.

Drugs that target ATP5F1EP2 may have potential therapeutic applications for a variety of mitochondrial disorders. For example, inhibitors of ATP5F1EP2 have been shown to be effective in treating certain forms of MELAS and in preventing neurodegeneration in animal models of certain neurodegenerative diseases. Additionally, drugs that target ATP5F1EP2 may be useful for treating certain types of cancer, as the H+ ATP synthase is a known drug target for many types of cancer.

Conclusion

ATP5F1EP2 is a protein that is involved in the production of ATP from Pi in the mitochondrial F1 complex. Its function as a catalytic subunit for the alpha subunit of H+ ATP synthase is critical for the function of the H+ ATP synthase and for the production of ATP . Mutations in the ATP5F1EP2 gene have been linked to various mitochondrial disorders, and drugs that target ATP5F1EP2 may have potential therapeutic applications for a variety of these disorders. Further research is needed to fully understand the role of ATP5F1EP2 in the production of ATP and to explore its potential as a drug target.

Protein Name: ATP Synthase F1 Subunit Epsilon Pseudogene 2

Functions: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity)

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