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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.7.7.15 dithiothreitol 20 mM Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.15 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
2.7.7.15 840000
-
 native PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.15 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.15 liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.7.15 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