EC Number   |
Reaction |
Reference |
|---|
   3.4.24.64 | Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 |
cleaves amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins |
-, 31389 |
| 3.4.24.64 | Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 |
limited proteolysis: cleaves precursors of mitochondrial proteins to their mature form, not further |
-, 31385 |
| 3.4.24.64 | Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 |
mechanism |
31396, 31400 |
| 3.4.24.64 | Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 |
release of N-terminal targeting peptides from precursor proteins imported into mitochondria typically with Arg in position P2 |
- |
| 3.4.24.64 | Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 |
structure-function relationship |
31394, 31400 |
| 3.4.24.64 | Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2 |
the amino acid residues on the C-terminal side of the cleavage site in the preprotein are orientated tail out from the large cavity of MPP and interact with the glycine-rich loop of the alpha-MPP subunit. Thus, MPP orientates preproteins at the specific cleft between the catalytic domain and the flexible glycine-rich loop, which seems to pinch the extended polypeptide, catalytic mechanism, overview |
683617 |
