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Literature summary for 2.7.7.15 extracted from

  • Cornell, R.
    Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase (1989), J. Biol. Chem., 264, 9077-9082.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol 20 mM Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
2 * 42000, SDS-PAGE, if bound to a detergent micelle or membrane vesicle the purified native enzyme is a dimer composed of two noncovalently linked 42000 MW subunits, in the absence of a membrane or micelle, the dimers self-aggregate in a reversible manner Rattus norvegicus
840000
-
native PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + choline phosphate
-
Rattus norvegicus diphosphate + CDPcholine
-
?

Subunits

Subunits Comment Organism
dimer 2 * 42000, SDS-PAGE, if bound to a detergent micelle or membrane vesicle the purified native enzyme is a dimer composed of two noncovalently linked 42000 MW subunits, in the absence of a membrane or micelle, the dimers self-aggregate in a reversible manner Rattus norvegicus