Recombinant Proteins
Product List
ATP5C1 Human
ATP Synthase Gamma Chain, Mitochondria Human Recombinant
ATP5C1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ATP5F1 Human
Synthase Transporting Mitochondrial Fo Complex B1 Human Recombinant
ATP5F1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (83-256) and having a molecular mass of 22.6 kDa. ATP5F1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ATP5H Human
ATP Synthase Mitochondrial Fo Complex Subunit D Human Recombinant
Introduction
ATP synthase is an enzyme that directly generates adenosine triphosphate (ATP) during cellular respiration. ATP is the primary energy molecule used in cells. ATP synthase forms ATP from adenosine diphosphate (ADP) and inorganic phosphate (Pi) through oxidative phosphorylation . ATP synthases are classified based on their functional differences into F (Phosphorylation Factor), V (Vacuole), A (Archaea), P (Proton), or E (Extracellular) ATPases . The mitochondrial ATP synthase is a multi-subunit protein complex with an approximate molecular weight of 550 kDa .
ATP synthase is a highly conserved enzyme found in various organisms, including bacteria, archaea, and eukaryotes . In eukaryotes, it is located in the inner mitochondrial membrane, while in prokaryotes, it is found in the plasma membrane . The enzyme consists of two main components: the membrane-bound F0 portion and the water-soluble F1 portion . The F0 region acts as a proton channel, while the F1 region is responsible for ATP synthesis . ATP synthase is ubiquitously expressed in tissues with high energy demands, such as muscle and brain tissues .
The primary function of ATP synthase is to produce ATP, which is essential for powering all cellular processes . ATP synthase maintains the electrochemical gradient generated by proton movement across the inner mitochondrial membrane . This gradient is crucial for other processes, such as nutrient transport and oxidative phosphorylation . Although ATP synthase is not directly involved in immune responses or pathogen recognition, the energy it produces is vital for the functioning of immune cells and other cellular processes .
ATP synthase operates through a rotational mechanism driven by the flow of protons across the inner mitochondrial membrane . The enzyme consists of two main parts: the F0 motor, which is embedded in the membrane, and the F1 motor, which protrudes into the mitochondrial matrix . Protons flow through the F0 region, causing it to rotate and drive the synthesis of ATP in the F1 region . This process is coupled with the electron transport chain, which generates the proton gradient .
ATP synthase activity is regulated by various mechanisms to ensure efficient ATP production . In mitochondria, the enzyme can be inactivated under low energy conditions by binding ADP-Mg to one of its catalytic sites . This inactive state can be reversed when energy levels increase . Additionally, the inhibitor protein IF1 can bind to ATP synthase under acidic conditions to prevent ATP hydrolysis . Post-translational modifications, such as phosphorylation, also play a role in regulating ATP synthase activity .
ATP synthase has several applications in biomedical research, diagnostics, and therapeutics . It is used as a target for studying mitochondrial diseases and developing drugs that modulate its activity . In diagnostics, ATP synthase activity can be measured to assess mitochondrial function in various diseases . Therapeutically, targeting ATP synthase can help in treating conditions like cancer, where mitochondrial function is often altered .
ATP synthase plays a crucial role throughout the life cycle, from development to aging and disease . During development, ATP synthase is essential for providing the energy required for cell growth and differentiation . In aging, mitochondrial dysfunction and reduced ATP synthase activity are associated with various age-related diseases . In diseases such as cancer, altered ATP synthase activity can contribute to the metabolic reprogramming of cancer cells .
