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Literature summary for 6.3.4.2 extracted from

  • Anderson, P.M.
    CTP synthetase from Escherichia coli: an improved purification procedure and characterization of hysteretic and enzyme concentration effects on kinetic properties (1983), Biochemistry, 22, 3285-3292.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
4 * 50000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.7
-
-
Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, purified enzyme is stable for months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + NH4+
-
Escherichia coli ADP + phosphate + CTP
-
?

Subunits

Subunits Comment Organism
More the enzyme can dissociate to an apparently inactive monomer. The dissociation is reversible and the rate of association is slow Escherichia coli
tetramer 4 * 50000, SDS-PAGE Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
reversible cold lability Escherichia coli