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Literature summary for 2.3.2.B11 extracted from

  • Majetschak, M.; Laub, M.; Jennissen, H.P.
    Q ubiquityl-calmodulin synthetase that effectively recognizes the Ca2+-free form of calmodulin (1993), FEBS Lett., 315, 347-352.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Oryctolagus cuniculus
Ca2+ during purification on ubiquitin-Sepharose the Ca2+-dependent activity is lost and an essentially Ca2+-independent enzyme is obtained which is purified 90fold Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
several possibly interdependent forms of uCaM-synthetase exist which display different specificities for calmodulin
-

Purification (Commentary)

Purification (Comment) Organism
during purification on ubiquitin-Sepharose the Ca2+-dependent activity is lost and an essentially Ca2+-independent enzyme is obtained which is purified 90fold Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
reticulocyte
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Oryctolagus cuniculus
0.0000192
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[RING-E3-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [calmodulin]-L-lysine several (possibly interdependent) forms of uCaM-synthetase exist which display different substrate specificities for calmodulin Oryctolagus cuniculus [RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
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