Based on limited published evidence, ZNG1F is a zinc chaperone that transfers zinc cofactor to target metalloproteins to activate them. It catalyzes zinc insertion into methionine aminopeptidase METAP1, which cleaves initiator methionine during protein translation 1. The N-terminal psi-PxLVp motif binds METAP1's zinc finger, followed by zinc transfer from ZNG1F's CXCC motif via GTP hydrolysis, with GTP/GDP exchange releasing active METAP1. Recent evidence indicates ZNG1F regulates intracellular zinc homeostasis, with suppression linked to mitochondrial dysfunction and oxidative stress in endothelial cells 2.