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Literature summary for 3.4.11.26 extracted from

  • Venne, A.S.; Voegtle, F.N.; Meisinger, C.; Sickmann, A.; Zahedi, R.P.
    Novel highly sensitive, specific, and straightforward strategy for comprehensive N-terminal proteomics reveals unknown substrates of the mitochondrial peptidase Icp55 (2013), J. Proteome Res., 12, 3823-3830.
    View publication on PubMed

Application

Application Comment Organism
analysis 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

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
additional information 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 ?
-
?

Synonyms

Synonyms Comment Organism
Icp55
-
Saccharomyces cerevisiae