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The collected fluorescent beads, which contained the hydrolysed peptides generated by<jats:italic>h<\/jats:italic>MIP, were sequenced by Edman degradation. The results showed that this peptidase presents a remarkable preference for polar uncharged residues at P<jats:sub>1<\/jats:sub> and P<jats:sub>1<\/jats:sub>\u2032 substrate positions: Ser = Gln &gt;Thr at P<jats:sub>1<\/jats:sub> and Ser &gt;Thr at P<jats:sub>1<\/jats:sub>\u2032. Non\u2010polar residues were frequent at the substrate P<jats:sub>3<\/jats:sub>, P<jats:sub>2<\/jats:sub>, P<jats:sub>2<\/jats:sub>\u2032 and P<jats:sub>3<\/jats:sub>\u2032 positions. Analysis of the predicted MIP processing sites in imported mitochondrial matrix proteins shows these cleavages indeed occur between polar uncharged residues. Previous analysis of these processing sites indicated the importance of positions far from the MIP cleavage site, namely the presence of a hydrophobic residue (Phe or Leu) at P<jats:sub>8<\/jats:sub> and a polar uncharged residue (Ser or Thr) at P<jats:sub>5<\/jats:sub>. To evaluate this, additional kinetic analyses were carried out, using fluorogenic substrates synthesized based on the processing sites attributed to MIP. The results described here underscore the importance of the P<jats:sub>1<\/jats:sub> and P<jats:sub>1<\/jats:sub>\u2032 substrate positions for the hydrolytic activity of<jats:italic>h<\/jats:italic>MIP. 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