3.4.24.64: mitochondrial processing peptidase
This is an abbreviated version!
For detailed information about mitochondrial processing peptidase, go to the full flat file.
Reaction
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
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Synonyms
Alpha-MPP, Atp23, Beta-MPP, EC 3.4.99.41, General mitochondrial processing peptidase, GPP, HA1523, HPP, Imp1, Imp2, inner membrane peptidase processing enzyme, Mas1, Mas2, Matrix peptidase, Matrix processing peptidase, Matrix processing proteinase, Mitochondrial chelator-sensitive protease, mitochondrial processing peptidase, mitochondrial processing peptidase-alpha protein, mitochondrial processing protease, Mitochondrial protein precursor-processing proteinase, MMP-beta, More, MPP, MPP-alpha, P-52, P-55, PEP, Plsp1, Plsp2, PMPCA, Processing enhancing peptidase, processing enhancing protein, processing peptidase, Proteinase, mitochondrial protein precursor-processing, thylakoidal processing peptidase, TPP, TTHA1264
ECTree
Reaction
Reaction on EC 3.4.24.64 - mitochondrial processing peptidase
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Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
mechanism
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Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
mechanism
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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
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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
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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
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Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
structure-function relationship
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Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
structure-function relationship
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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
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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
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-
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
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