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Literature summary for 2.3.2.B11 extracted from

  • Majetschak, M.; Laub, M.; Meyer, H.E.; Jennissen, H.P.
    The ubiquityl-calmodulin synthetase system from rabbit reticulocytes: isolation of the ubiquitin-binding first component, a ubiquitin-activating enzyme (1998), Eur. J. Biochem., 255, 482-491.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
111600
-
2 * 111600, SDS-PAGE Oryctolagus cuniculus
111975
-
2 * 111975, calculation from nucleotide sequence Oryctolagus cuniculus
112140
-
2 * 112140, electrospray ion mass spectrometry Oryctolagus cuniculus
213000
-
gel filtration Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of the holoenzyme system uCaM synthetase. Fractionation yields two essentially inactive components: uCaM Syn-F1 and uCaM Syn-F2 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
0.0001218
-
uCaM synthetase Oryctolagus cuniculus
0.0396
-
uCaM Syn-F1 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
-
Oryctolagus cuniculus [RING-E3-ubiquitin-carrier protein]-L-cysteine + [calmodulin]-N6-ubiquitinyl-L-lysine
-
?

Subunits

Subunits Comment Organism
dimer 2 * 111975, calculation from nucleotide sequence Oryctolagus cuniculus
dimer 2 * 112140, electrospray ion mass spectrometry Oryctolagus cuniculus
dimer 2 * 111600, SDS-PAGE Oryctolagus cuniculus