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Literature summary for 3.4.19.1 extracted from

  • Palmieri, G.; Bergamo, P.; Luini, A.; Ruvo, M.; Gogliettino, M.; Langella, E.; Saviano, M.; Hegde, R.N.; Sandomenico, A.; Rossi, M.
    Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation (2011), PLoS One, 6, e25888.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
(10E,12Z)-octadeca-10,12-dienoic acid non-competitive inhibition mechanism Saccharolobus solfataricus
peptide SsCEI 2 specific and efficient inhibition. No inhibition in presence of peptide SsCEI 3 and peptide SsCEI 4 Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Leu-4-nitroanilide + H2O
-
Saccharolobus solfataricus N-acetyl-Leu + 4-nitroaniline
-
?

Synonyms

Synonyms Comment Organism
acylpeptide hydrolase
-
Saccharolobus solfataricus
APEHs
-
Saccharolobus solfataricus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.001
-
peptide SsCEI 2 pH 7.5, 37°C Saccharolobus solfataricus
0.14
-
(10E,12Z)-octadeca-10,12-dienoic acid pH 7.5, 37°C Saccharolobus solfataricus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.01
-
pH 7.5, 37°C Saccharolobus solfataricus peptide SsCEI 2
0.08
-
pH 7.5, 37°C Saccharolobus solfataricus (10E,12Z)-octadeca-10,12-dienoic acid