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Literature summary extracted from

  • Laub, M.; Steppuhn, J.A.; Bluggel, M.; Immler, D.; Meyer, H.E.; Jennissen, H.P.
    Modulation of calmodulin function by ubiquitin-calmodulin ligase and identification of the responsible ubiquitylation site in vertebrate calmodulin (1998), Eur. J. Biochem., 255, 422-431.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.B11 additional information removal of the 41 C-terminal amino acids (fourth Ca2+-binding loop) separated by several nanometers from Lys21 drastically decreases the affinity and reactivity of the synthetase for calmodulin Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.B11 additional information
-
 additional information
-
 Oryctolagus cuniculus
2.3.2.B11 0.0009
-
 Calmodulin calmodulin from paramecium tetraurelia Oryctolagus cuniculus
2.3.2.B11 0.0013
-
 Calmodulin calmodulin from Xenopus laevis Oryctolagus cuniculus
2.3.2.B11 0.0049
-
 Calmodulin calmodulin from bovine testis Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.B11 Ca2+ required Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.B11 n ATP + calmodulin + n ubiquitin Oryctolagus cuniculus monoubiquitylation strongly decreases the biological activity of calmodulin towards phosphorylase kinase by reducing its affinity approximately threefold and the maximal degree of activation approximately twofold ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.B11 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.B11 reticulocyte
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.B11 n ATP + calmodulin + n ubiquitin monoubiquitylation strongly decreases the biological activity of calmodulin towards phosphorylase kinase by reducing its affinity approximately threefold and the maximal degree of activation approximately twofold Oryctolagus cuniculus ?
-
 ?
2.3.2.B11 [RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine calmodulin from bovine testis, Xenopus laevis or Paramecium tetraurelia. Paramecium calmodulin which is dimethylated at Lys13 is an efficient susbstrate Oryctolagus cuniculus [RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
 ?
2.3.2.B11 [RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine the ubiquitylation site has the octapeptide structure -L-F-D-K21-D-G-D-G- with Lys21 being the ubiquitylated residue in vertebrate and other calmodulins. Removal of the 41 C-terminal amino acids (fourth Ca2+-binding loop) separated by several nanometers from Lys21 drastically decreases the affinity and reactivity of the synthetase for calmodulin. The nearly identical site -V-F-D-K94-D-G-N-G- in the third Ca2+-binding loop of vertebrate calmodulin is apparently not ubiquitylated by the synthetase Oryctolagus cuniculus [RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
 ?