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Literature summary for 3.4.19.12 extracted from

  • Melandri, F.; Grenier, L.; Plamondon, L.; Huskey, W.P.; Stein, R.L.
    Kinetic studies on the inhibition of isopeptidase T by ubiquitin aldehyde (1996), Biochemistry, 35, 12893-12900.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ubiquitin submicromolar concentrations activate while higher concentrations inhibit the enzyme, regulatory function, binding via 2 ubiquitin binding sites extending the active site Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
ubiquitin submicromolar concentrations activate while higher concentrations inhibit the enzyme, regulatory function, 2-step inhibition mechanism via 2 ubiquitin binding sites extending the active site Oryctolagus cuniculus
Ubiquitin aldehyde inhibition in absence of ubiquitin, competitive to ubiquitin Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
reticulocyte
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
polyubiquitin + H2O
-
Oryctolagus cuniculus ubiquitin
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Oryctolagus cuniculus
0.0000001
-
ubiquitin-aldehyde at 0.0006 mM ubiquitin, pH 7.8, 25°C Oryctolagus cuniculus
0.0000023
-
ubiquitin-aldehyde in absence of ubiquitin, pH 7.8, 25°C Oryctolagus cuniculus