ATP5F1C: The Key Enzyme for Cellular Energy Synthesis (G509)

Target Name: ATP5F1C

NCBI ID: G509

ATP5F1C

ATP5F1C: The Key Enzyme for Cellular Energy Synthesis

ATP5F1C, also known as ATP synthase subunit gamma, is a protein that is found in the mitochondria. It plays a critical role in the production of ATP, which is the energy currency of the cell. ATP is essential for all cellular processes, including muscle contractions, nerve impulses, and metabolism. The process of synthesizing ATP is called the intracellular ATP synthesis pathway. This process involves the participation of multiple enzymes, among which ATP synthase is one of the key enzymes. ATP synthase is divided into two forms, ATP synthase alpha and ATP synthase beta. ATP synthase beta is also called ATP synthase beta.

ATP5F1C is the main component of the 尾 subunit of ATP synthase. ATP synthase 尾 consists of two subunits 伪尾. Each subunit contains an ATP synthase active center, which is a key region for ATP synthesis. ATP5F1C is an important active center in the 尾 subunit of ATP synthase.

ATP5F1C has multiple biological functions. First, ATP5F1C is the main component of the 尾 subunit of ATP synthase, so it plays an important role in the synthesis of ATP. Secondly, ATP5F1C can bind a variety of substrates, including FAD, NAD+ and CoQ. These conjugates are necessary for the ATP synthesis pathway. Finally, ATP5F1C has additional functions in cellular metabolism. For example, it can regulate intracellular cholesterol levels, participate in apoptosis, and can affect intracellular signaling.

ATP5F1C has broad application prospects in drug research and treatment. Since ATP is the most commonly used energy supplier within cells, any drug that affects the ATP synthesis pathway may have effects on the cell. Many drugs, including antibiotics, antidepressants, and antihypertensives, act on the ATP synthesis pathway, thereby affecting cell function. In addition, ATP5F1C can also be used as a potential drug to treat cancer. Cancer cells often have high ATP needs, so inhibitors of the ATP synthesis pathway can inhibit cancer cell growth and spread.

The molecular structure of ATP5F1C also plays a key role in its function. ATP5F1C has a unique glycosylation pattern. The N-terminus of ATP5F1C contains an 伪-helix, which is a characteristic in the 尾 subunit of ATP synthase. In addition, the C-terminus of ATP5F1C contains a 尾-sheet, which is also one of the characteristics of the 尾 subunit of ATP synthase. These structural features enable ATP5F1C to bind a variety of substrates, including FAD, NAD+, and CoQ.

ATP5F1C may also serve as a potential drug for the treatment of cancer. Cancer cells often have high ATP needs, so inhibitors of the ATP synthesis pathway can inhibit cancer cell growth and spread. For example, studies have shown that ATP synthesis inhibitors can inhibit the proliferation and metastasis of cancer cells. In addition, ATP5F1C could be used to treat other diseases, such as heart disease and neurological disorders.

ATP5F1C is a protein that plays an important role in cellular metabolism. It has an important impact on the ATP synthesis pathway and can be used as a potential target for drug research and treatment. With the deepening of research, ATP5F1C will become an important drug target for the treatment of various diseases.

Protein Name: ATP Synthase F1 Subunit Gamma

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 the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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

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