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Literature summary extracted from

  • Ding, Z.; Taneva, S.G.; Huang, H.K.; Campbell, S.A.; Semenec, L.; Chen, N.; Cornell, R.B.
    A 22-mer segment in the structurally pliable regulatory domain of metazoan CTP:phosphocholine cytidylyltransferase facilitates both silencing and activating functions (2012), J. Biol. Chem., 287, 38980-38991.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.15 additional information creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Caenorhabditis elegans, the tail domain of the invertebrate CCT is competent for both suppression of catalytic activity and for activation by lipid vesicles Caenorhabditis elegans
2.7.7.15 additional information creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Drosophila melanogaster, the tail domain of the invertebrate CCT is competent for both suppression of catalytic activity and for activation by lipid vesicles Drosophila melanogaster
2.7.7.15 additional information creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Saccharomyces cerevisiae Saccharomyces cerevisiae
2.7.7.15 additional information creation of chimeric enzymes by fusing the catalytic domain of rat CCTalpha to the regulatory tail of CCTs from Drosophila melanogaster, Caenorhabditis elegans, or Saccharomyces cerevisiae or to alpha-synuclein. Deletion of the a highly amphipathic 22-residue segment in the membrane-inducible amphipathic helix increased the lipid-independent Vmax by 10fold, equivalent to the effect of deleting the entire tail, and severely weakened membrane binding affinity, but membrane binding is required for additional increases in catalytic efficiency. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.15 Caenorhabditis elegans
-
-
-
2.7.7.15 Drosophila melanogaster
-
-
-
2.7.7.15 Rattus norvegicus
-
-
-
2.7.7.15 Saccharomyces cerevisiae
-
-
-

Subunits

EC Number Subunits Comment Organism
2.7.7.15 More the enzyme is composed of a catalytic head domain and a regulatory tail Drosophila melanogaster
2.7.7.15 More the enzyme is composed of a catalytic head domain and a regulatory tail Rattus norvegicus
2.7.7.15 More the enzyme is composed of a catalytic head domain and a regulatory tail Saccharomyces cerevisiae
2.7.7.15 More the enzyme is composed of a catalytic head domain and a regulatory tail Caenorhabditis elegans

Synonyms

EC Number Synonyms Comment Organism
2.7.7.15 CCT
-
 Drosophila melanogaster
2.7.7.15 CCT
-
 Rattus norvegicus
2.7.7.15 CCT
-
 Saccharomyces cerevisiae
2.7.7.15 CCT
-
 Caenorhabditis elegans
2.7.7.15 CTP:phosphocholine cytidylyltransferase
-
 Drosophila melanogaster
2.7.7.15 CTP:phosphocholine cytidylyltransferase
-
 Rattus norvegicus
2.7.7.15 CTP:phosphocholine cytidylyltransferase
-
 Saccharomyces cerevisiae
2.7.7.15 CTP:phosphocholine cytidylyltransferase
-
 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
2.7.7.15 additional information 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 Rattus norvegicus
2.7.7.15 additional information 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 Drosophila melanogaster
2.7.7.15 additional information 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 Saccharomyces cerevisiae
2.7.7.15 additional information 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 Caenorhabditis elegans
2.7.7.15 physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Drosophila melanogaster
2.7.7.15 physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Rattus norvegicus
2.7.7.15 physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Saccharomyces cerevisiae
2.7.7.15 physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Caenorhabditis elegans