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Literature summary for 3.4.11.26 extracted from

  • Huang, S.; Nelson, C.J.; Li, L.; Taylor, N.L.; Stroeher, E.; Peteriet, J.; Millar, A.H.
    Intermediate claevage peptidase55 modifies enzyme amino termini and alters protein stability in Arabidopsis mitochondria (2015), Plant Physiol., 168, 415-427 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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Arabidopsis thaliana 5739
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana F4HZG9
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SSLPSEAVDEK + H2O N-terminal peptide of protein At4g37930 Arabidopsis thaliana SLPSEAVDEK + Ser
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?

General Information

General Information Comment Organism
physiological function ICP55 is responsible for the removal of single N-terminal amino acids, and its action explained the -3 arginine processing motif of a number of mitochondrial proteins. ICP55 also removes single amino acids from mitochondrial proteins known to be cleaved at nonconserved arginine sites. Disruption of ICP55 alters mitochondrial protein stability in vitro and changes the protein turnover rate of selected proteins in vivo Arabidopsis thaliana