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Literature summary for 2.3.2.B11 extracted from

  • Parag, H.A.; Dimitrovsky, D.; Raboy, B.; Kulka, R.G.
    Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae (1993), FEBS Lett., 325, 242-246.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information calmodulin is not ubiquitinated by the enzyme unless E1 and UBC4 are present Saccharomyces cerevisiae
additional information weak, but distinct activity is observed when UBC4 is replaced by UBC1 Saccharomyces cerevisiae
additional information traces of activity are also observed when RAD6 replaces UBC4 Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
EGTA
-
Saccharomyces cerevisiae
Trifluoperazine 0.03 mM Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with beta-lactoglobulin, beta-casein, kappa-casein, alpha-casein and oxidized ribonuclease Saccharomyces cerevisiae ?
-
?
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine specific for calmodulin Saccharomyces cerevisiae [RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
?