Mitochondrial processing peptidase (MPP) is a soluble enzyme complex which cleaves N-terminal signal sequences from mitochondrial preproteins after translocation the double membrane. MPP can also cleave the N-terminal presequences followed by hydrophobic sorting signals in proteins localized in the inner membrane and intermembrane space. MMP is a dimeric complex, with an alpha subunit which binds the presequence and a catalytic beta subunit. (Adapted from PMID:22172993 and PMID:35185991.)

signal peptidase I (3.4.21.89)

neprilysin (3.4.24.11)

procollagen N-endopeptidase (3.4.24.14)

stromelysin 1 (3.4.24.17)

meprin A (3.4.24.18)

procollagen C-endopeptidase (3.4.24.19)

astacin (3.4.24.21)

stromelysin 2 (3.4.24.22)

matrilysin (3.4.24.23)

gelatinase A (3.4.24.24)

microbial collagenase (3.4.24.3)

neutrophil collagenase (3.4.24.34)

gelatinase B (3.4.24.35)

saccharolysin (3.4.24.37)

pitrilysin (3.4.24.55)

insulysin (3.4.24.56)

O-sialoglycoprotein endopeptidase (3.4.24.57)

mitochondrial intermediate peptidase (3.4.24.59)

nardilysin (3.4.24.61)

mitochondrial processing peptidase (3.4.24.64)

macrophage elastase (3.4.24.65)

bontoxilysin (3.4.24.69)

interstitial collagenase (3.4.24.7)

oligopeptidase A (3.4.24.70)

endothelin-converting enzyme 1 (3.4.24.71)

fibrolase (3.4.24.72)