Hydrolases;
Acting on peptide bonds (peptidases);
Aminopeptidases
BRITE hierarchy

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.

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.

EC 3.4.11.26 created 2011

1  [PMID:19720832]

Naamati A, Regev-Rudzki N, Galperin S, Lill R, Pines O

Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55.

J Biol Chem 284:30200-8 (2009)
DOI:10.1074/jbc.M109.034694

[sce:YER078C]

2  [PMID:19837041]

Vogtle FN, Wortelkamp S, Zahedi RP, Becker D, Leidhold C, Gevaert K, Kellermann J, Voos W, Sickmann A, Pfanner N, Meisinger C

Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability.

Cell 139:428-39 (2009)
DOI:10.1016/j.cell.2009.07.045

[sce:YER078C]