EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.11.26 | FSTPSDLDSELTR + H2O |
N-terminal peptide of protein Oxa1 |
Arabidopsis thaliana |
STPSDLDSELTR + Phe |
- |
? |
3.4.11.26 | FTSEAAADGGQDQILSR + H2O |
N-terminal peptide of mitochondrial acyl carrier protein 3 |
Arabidopsis thaliana |
TSEAAADGGQDQILSR + Phe |
- |
? |
3.4.11.26 | Isa2 + H2O |
- |
Saccharomyces cerevisiae |
? |
substrate is likely processed by isoform Icp55 in two consecutive steps, in which Icp55 removes two destabilizing amino acids: first Phe and then in a second round of processing Tyr, resulting in the mature stable protein |
? |
3.4.11.26 | Met-Pro-Ala + H2O |
- |
Saccharomyces cerevisiae |
Met + Pro-Ala |
- |
? |
3.4.11.26 | more |
Icp55 is critical for stabilization of the mitochondrial proteome. Icp55 removes an amino acid from a characteristic set of N-termini of preprotein intermediates generated by mitochondrial processing peptidase. Thereby Icp55 converts instable intermediates into stable proteins |
Saccharomyces cerevisiae |
? |
- |
? |
3.4.11.26 | more |
global analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins. The N-proteome of icp55DELTA mitochondria yielded proteins whose N-terminus differs by one residue from the mature N-terminus of wild-type mitochondria. Icp55 cleaves between the last amino acid of the presequence (tyrosine, leucine or phenylalanine) and the first residue of the mature protein, preferentially serine, alanine and threonine. The most frequent residue tyrosine is efficiently removed by Icp55 and thus is the best substrate of Icp55. The efficiency of cleavage is lower for leucine and phenylalanine |
Saccharomyces cerevisiae |
? |
- |
? |
3.4.11.26 | more |
identification of 36 substrates utilizing charge-based fractional diagonal chromatography, enabling the differential quantitation of 1459 nonredundant N-terminal peptides between two Saccharomyces cerevisiae samples within 10 h of LC-MS, starting from only 50 microg of protein per condition and analyzing only 40% of the obtained fractions |
Saccharomyces cerevisiae |
? |
- |
? |
3.4.11.26 | more |
enzyme is able to remove N-terminal amino acids L, Y, I, F, C, M of mitochondrial proteins |
Arabidopsis thaliana |
? |
- |
? |
3.4.11.26 | more |
residue Tyr is preferred at P1 position. The enzyme additionally displays Xaa-Pro aminopeptidase activity in vitro |
Saccharomyces cerevisiae |
? |
- |
? |
3.4.11.26 | more |
the enzyme is active towards substrates with proline at P1' position (M-/-PA and Y-/-PA). Icp55 cleaves off bulky residues from N-termini of proteins. Active towards substrates Y-/-AA, Y-/-TA and Y-/-SA |
Saccharomyces cerevisiae |
? |
- |
? |