Mitochondrial intermediate peptidase
| Mitochondrial intermediate peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.59 | ||||||||
| CAS number | 136447-30-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Mitochondrial intermediate peptidase (EC 3.4.24.59, mitochondrial intermediate precursor-processing proteinase, MIP) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion
This enzyme is a homologue of thimet oligopeptidase.
References
- ↑ Isaya, G.; Kalousek, F.; Rosenberg, L.E. (1992). "Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase". J. Biol. Chem. 267: 7904–7910. PMID 1560019.
- ↑ Isaya, G.; Kalousek, F.; Rosenberg, L.E. (1992). "Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue". Proc. Natl. Acad. Sci. USA. 89: 8317–8321. doi:10.1073/pnas.89.17.8317. PMID 1518864.
External links
- Mitochondrial intermediate peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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