EC Number   |
General Information |
Reference |
|---|
    2.7.7.15 | metabolism |
rate-limiting enzyme of the lipid biosynthesis pathway |
762455 |
| 2.7.7.15 | metabolism |
the enzyme catalyzes a step in the Kennedy pathway for phosphatidylecholine synthesis, overview |
721989 |
| 2.7.7.15 | metabolism |
the enzyme catalyzes conversion of phosphocholine and CTP to cytidine diphosphocholine (CDP-choline), a step critical for synthesis of the membrane phospholipid phosphatidylcholine |
737438 |
| 2.7.7.15 | metabolism |
the enzyme catalyzes the formation of CDP-choline, a key intermediate in the choline branch of the Kennedy pathway |
762463 |
| 2.7.7.15 | more |
the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding |
722793 |
| 2.7.7.15 | more |
the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan |
722793 |
| 2.7.7.15 | physiological function |
CTP:phosphocholine cytidylyltransferase alpha is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine synthesis. Lipid activation of the enzyme results in its translocation to the nuclear envelope and expansion of an intranuclear membrane network termed the nucleoplasmic reticulum by a mechanism involving membrane deformation. CCTalpha and lamins specifically cooperate to form the nucleoplasmic reticulum, but the overall structure of the nuclear envelope has a minimal impact on enzyme activity and phosphocholine synthesis |
721712 |
| 2.7.7.15 | physiological function |
CTP:phosphocholine cytidylyltransferase alpha is a nuclear enzyme that catalyzes the rate-limiting step in the CDP-choline pathway for phosphatidylcholine synthesis. The enzyme is not involved in the Hutchinson-Gilford progeria syndrome, overview |
721712 |
| 2.7.7.15 | physiological function |
CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis |
722793 |
| 2.7.7.15 | physiological function |
CTP:phosphocholine cytidylyltransferase-alpha (CCTalpha) and CCTbeta catalyze the rate limiting step in phosphatidylcholine biosynthesis |
761872 |
