The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: mitochondrial processing peptidase
Reaction: Release of N-terminal targetting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2
Other name(s): processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; MPP
Comments: Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin [3], and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 86280-61-7
1.  Jensen, R.E. and Yaffe, M.P. Import of proteins into yeast mitochondria: the nuclear MAS2 gene encodes a component of the processing protease that is homologous to the MAS1-encoded subunit. EMBO J. 7 (1988) 3863–3871. [PMID: 3061808]
2.  Witte, C., Jensen, R.E., Yaffe, M.P. and Schatz, G. MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease. EMBO J. 7 (1988) 1439–1447. [PMID: 3044780]
3.  Rawlings, N.D. and Barrett, A.J. Homologues of insulinase, a new superfamily of metalloendopeptidases. Biochem. J. 275 (1991) 389–391. [PMID: 2025223]
4.  Kalousek, F., Neupert, W., Omura, T., Schatz, G. and Schmitz, U.K. Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins. Trends Biochem. Sci. 18 (1993) 249. [DOI] [PMID: 8212133]
5.  Brunner, M. and Neupert, W. Purification and characterization of the mitochondrial processing peptidase of Neurospora crassa. Methods Enzymol. 248 (1994) 717–728.
[EC created 1989/90 as EC, transferred 1995 to EC]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald