EC Number   |
Natural Substrates |
|---|
   3.4.24.64 | more |
the enzyme genetically interacts with prohibitins in the inner mitochondrial membrane and links the function of prohibitins to the F1FO-ATP synthase complex |
| 3.4.24.64 | more |
the enzyme specifically recognizes mitochondrial preproteins and removes their basic N-terminal signal prepeptides |
| 3.4.24.64 | more |
the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview |
| 3.4.24.64 | more |
cleavage site specificity of the major mitochondrial processing peptidase for removal of N-terminal presequences from mitochondrial proteins during maturation, global analysis of the N-proteome of yeast mitochondria, method, overview. For a number of proteins such as Gif1 and Pdb1, more than one N-terminus exist, therefore two truncated versions of the proteins are synthesized and compared to the in organello processing product, product identification by LC-MS/MS analysis |
| 3.4.24.64 | more |
isoform Plsp1 forms a stable complex with PGRL1 in Arabidopsis thylakoids |
| 3.4.24.64 | more |
the enzyme specifically cleaves off presequences from mitochondrial precursor proteins |
| 3.4.24.64 | Nfs1 + H2O |
MPP cleaves the precursor between Phe33 and Tyr34, Nfs1 processing, overview |
| 3.4.24.64 | nuclear-encoded polyprotein precursor + H2O |
the nuclear-encoded protein RPS14 (ribosomal protein S14) of rice mitochondria is synthesized in the cytosol as a polyprotein consisting of a large N-terminal domain comprising preSDHB (succinate dehydrogenase B precursor) and the C-terminal RPS14. After the preSDHBRPS14 polyprotein is transported into the mitochondrial matrix, the protein is processed into three peptides: the N-terminal prepeptide, the SDHB domain and the C-terminal mature RPS14. MPP (mitochondrial processing peptidase) plays an essential role in processing of the polyprotein. Purified yeast MPP cleaves both the N-terminal presequence and the connector region between SDHB and RPS14. The connector region is processed more rapidly than the presequence. The cleavage site between SDHB and RPS14 is located in an MPPprocessing motif. MPP interacts with multiple sites in the region, possibly in a similar manner to the interaction with the N-terminal presequence. In addition, MPP preferentially recognizes the unfolded structure of preSDHBRPS14. In mitochondria, MPP may recognize the stretched poly-protein during passage of the precursor through the translocational apparatus in the inner membrane, and cleaves the connecting region between the SDHB and RPS14 domains even before processing of the presequence |
| 3.4.24.64 | pea glutathione reductase + H2O |
signal peptide is cleaved off by the mitochondrial processing peptidase. Removal of 30 N-terminal amino acid residues of the signal peptide (GRD130) greatly stimulates processing activity. Constructs with a deletion of an additional ten amino acid residues (GRD140) and deletion of 22 amino acid residues in the middle of the GR signal sequence (GRD3052) are not celeaved by MPP. Mutations within two amino acid residues on either side of the processing site have inhibitory effect on processing by MPP with a nearly complete inhibition for mutations at position K1. Mutation of positively charged residues in the C-terminal half of the GR targeting peptide inhibit processing by MPP |
| 3.4.24.64 | phosphatase and tensin homologue-induced kinase 1 + H2O |
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