ExplorEnz: EC 3.4.11.26

Your query returned 1 entry. Printable version

3.4.11.26

Accepted name:

intermediate cleaving peptidase 55

Reaction:

The enzyme cleaves the Pro³⁶-Pro³⁷ bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.

Other name(s):

Icp55; mitochondrial intermediate cleaving peptidase 55 kDa

Comments:

Icp55 removes the destabilizing N-terminal amino acid residues that are left after cleavage by the mitochondrial processing peptidase, leading to the stabilisation of the substrate. The enzyme can remove single amino acids or a short peptide, as in the case of cysteine desulfurase (EC 2.8.1.7), where three amino acids are removed.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB

References:

1.	Naamati, A., Regev-Rudzki, N., Galperin, S., Lill, R. and Pines, O. Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J. Biol. Chem. 284 (2009) 30200–30208. [DOI] [PMID: 19720832]
2.	Vogtle, F.N., Wortelkamp, S., Zahedi, R.P., Becker, D., Leidhold, C., Gevaert, K., Kellermann, J., Voos, W., Sickmann, A., Pfanner, N. and Meisinger, C. Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability. Cell 139 (2009) 428–439. [DOI] [PMID: 19837041]

[EC 3.4.11.26 created 2011]