ATP synthase F1 subunit alpha, mitochondrial (ATP5F1A)

ATP synthase F1 subunit alpha, mitochondrial (ATP5F1A), is a nuclear-encoded subunit of mitochondrial ATP synthase (Complex V), located in the inner mitochondrial membrane as part of the F1 sector of the enzyme complex[2][1]. It functions as a key structural component of the catalytic core that drives the synthesis of ATP from ADP and inorganic phosphate during oxidative phosphorylation[2][1][3]. The F1 sector consists of three alpha and three beta subunits, forming a hexamer; while the beta subunits catalyze ATP formation, the alpha subunits provide structural and regulatory roles and are essential for nucleotide binding but are not the primary catalytic sites[4][1]. Mutations in ATP5F1A cause mitochondrial diseases including combined oxidative phosphorylation deficiency 22 (COXPD22) and mitochondrial complex V deficiency (MC5DN4), leading to diverse symptoms ranging from neurodevelopmental disorders to cardiomyopathy and encephalopathy[2]. ATP synthase is a fundamental enzyme universally required for cellular energy metabolism. Inhibitors of this complex, such as oligomycin, are primarily research tools due to the enzyme's systemic importance and associated safety risks in therapeutic targeting[2][1].

Other names

ATP synthase F(1) complex subunit alpha, mitochondrialATP5AATP5A1ATP5AL2ATPMCOXPD22HEL-S-123mMC5DN4MC5DN4AMC5DN4BMOM2OMRORMhATP1ATP synthase alpha chain, mitochondrialATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1

Enzyme inhibition (e.g., oligomycin inhibits proton flow, halting ATP synthesis); Modulation of catalytic activity (e.g., resveratrol inhibits F1 core, leading to increased AMP and activation of AMPK)[2]