Mitochondrial intermediate peptidase
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| Mitochondrial intermediate peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.59 | ||||||||
| CAS no. | 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 LE (April 1992). "Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase". The Journal of Biological Chemistry. 267 (11): 7904–10. doi:10.1016/S0021-9258(18)42598-7. PMID 1560019.
- ^ Isaya G, Kalousek F, Rosenberg LE (September 1992). "Sequence analysis of rat mitochondrial intermediate peptidase: similarity to zinc metallopeptidases and to a putative yeast homologue". Proceedings of the National Academy of Sciences of the United States of America. 89 (17): 8317–21. doi:10.1073/pnas.89.17.8317. PMC 49909. PMID 1518864.
External links
- Mitochondrial+intermediate+peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
