ATP synthase subunit C lysine N-methyltransferase (ATPSCKMT)

ATP synthase subunit C lysine N-methyltransferase (ATPSCKMT) is a mitochondrial enzyme responsible for trimethylating specific lysine residues on ATP synthase subunit C (notably ATP5MC1 and ATP5MC2)[2][6]. This post-translational modification is required for proper assembly of ATP synthase, supporting mitochondrial bioenergetics and cellular respiration[2][6][3]. Genetic disruption or deficiency of ATPSCKMT reduces ATP production, impairs mitochondrial function, and has been implicated in disorders such as retinal macular dystrophy and cardiovascular defects[3]. Additionally, enhanced activity in sensory neurons promotes persistent inflammatory and neuropathic pain by increasing reactive oxygen species and activating spinal cord microglia[3]. ATPSCKMT is also associated with neurodegenerative disease pathophysiology due to its role in mitochondrial protein homeostasis and pain signaling[1][3]. No drugs currently target this enzyme directly, and it is an emerging therapeutic target for pain modulation and mitochondrial disease[3][6].

Other names

FAM173BhFAM173BJS-2Protein N-lysine methyltransferase FAM173Bfamily with sequence similarity 173 member BACKMT

Inhibiting or modulating trimethylation of ATP synthase subunit C (no approved drugs known; mechanism predicted by methyltransferase inhibition)