This recombinant protein product features a stable and soluble 457-amino acid fragment (residues 317-773) of human ATP-dependent zinc metalloprotease YME1L1, designed for structural and biochemical studies. YME1L1 is a key mitochondrial enzyme involved in protein degradation and mitochondrial quality control, making this fragment an essential tool for investigating its mechanisms and interactions.

YME1L1 is an ATP-dependent metalloprotease located in the mitochondrial inner membrane, crucial for maintaining mitochondrial integrity and function. It degrades both folded and unfolded proteins within the mitochondrial intermembrane space, playing a vital role in regulating mitochondrial morphology by cleaving OPA1 to support normal structure and protein metabolism. The enzyme ensures cell proliferation, maintains cristae morphology, and promotes antiapoptotic activity by controlling the accumulation of nonassembled respiratory chain subunits and oxidatively damaged proteins. Additionally, YME1L1 adapts m