EC Number   |
General Information |
Reference  |
|---|
   3.4.24.64 | physiological function |
the mitochondrial processing protease is required in maturation of mitochondrial proproteins for removal of the N-terminal presequences |
708076 |
| 3.4.24.64 | metabolism |
yeast Nfs1 undergoes two steps of proteolytic processing: first it is cleaved by the mitochondrial processing peptidase, MPP, which removes its mitochondrial targeting sequence, and then it is cleaved by a peptidase, designated Icp55, which removes three amino acids from its N-terminus |
709066 |
| 3.4.24.64 | more |
expression of mppA is developmentally regulated |
709853 |
| 3.4.24.64 | physiological function |
MPP plays an essential role in mitochondrial biogenesis and cell proliferation |
709853 |
| 3.4.24.64 | physiological function |
MPP is involved in the transport of nuclear-encoded proteins from the cytosol into mitochondria |
-, 710508 |
| 3.4.24.64 | malfunction |
reducing enzyme activity induces phosphatase and tensin homologue-induced kinase 1 accumulation at the mitochondrial surface, leading to Parkin recruitment and mitophagy |
733730 |
| 3.4.24.64 | metabolism |
the enzyme plays a role in phosphatase and tensin homologue-induced kinase 1 (PINK1) import and mitochondrial quality control via the PINK1-Parkin pathway |
733730 |
| 3.4.24.64 | metabolism |
the thylakoid-transfer signal is required for energy-dependent translocation of preproteins into the thylakoid lumen and is removed by the thylakoidal processing peptidase |
733864 |
| 3.4.24.64 | malfunction |
ablation of the enzyme not only affects processing of mitochondrial matrix proteins but also inhibits the import process itself |
734654 |
| 3.4.24.64 | physiological function |
primary enzyme responsible for the maturation of the vast majority of nuclear-encoded mitochondrial proteins, which is necessary for life at the cellular level. Analysis of lymphoblastoid cells and fibroblasts from patients homozygous for the PMPCA p.Ala377Thr, a mutation in the alpha subunit of mitochondrial processing peptidase and carriers demonstrate that the mutation impacts both the level of the alpha subunit encoded by PMPCA and the function of mitochondrial processing peptidase. This mutation impacts the maturation process of frataxin, the protein which is depleted in Friedreich ataxia |
753119 |
