MAP1D is localized in the mitochondria and plays a crucial role in the N-terminal methionine excision pathway . This pathway involves the removal of the N-terminal methionine from many proteins, facilitating subsequent protein modifications . The enzyme requires the deformylation of the N(alpha)-formylated initiator methionine before it can hydrolyze the methionine .
The activity of MAP1D is essential for cell growth and viability . It has been observed that MAP1D is over-expressed in colon cancer cell lines and colon tumors, suggesting a potential role in tumorigenesis . The enzyme’s ability to remove methionine from nascent proteins is critical for maintaining cellular homeostasis and function .
Recombinant Human Methionine Aminopeptidase 1D is produced using baculovirus expression systems in Spodoptera frugiperda (Sf 21) cells . The recombinant protein typically includes an N-terminal methionine and a C-terminal 10-His tag for purification purposes . The protein is supplied as a 0.2 μm filtered solution in Tris, NaCl, and Glycerol, and is shipped with polar packs to maintain stability .